Rees, Douglas

Article from CaltechAUTHORS

• Warmack, Rebeccah A. and Rees, Douglas C. (2024) Structural evolution of nitrogenase states under alkaline turnover; Nature Communications; Vol. 15; No. 1; 10472; PMCID PMC11612016; 10.1038/s41467-024-54713-0
• Heidinger, Lorenz and Perez, Kathryn, el al. (2024) Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra; Nature Communications; Vol. 15; 4041; PMCID PMC11091149; 10.1038/s41467-024-48271-8
• Warmack, Rebeccah A. and Wenke, Belinda B., el al. (2024) Anaerobic cryoEM protocols for air-sensitive nitrogenase proteins; Nature Protocols; 10.1038/s41596-024-00973-5
• Warmack, Rebeccah A. and Rees, Douglas C. (2023) Nitrogenase beyond the Resting State: A Structural Perspective; Molecules; Vol. 28; No. 24; 7952; PMCID PMC10745740; 10.3390/molecules28247952
• Warmack, Rebeccah A. and Maggiolo, Ailiena O., el al. (2023) Structural consequences of turnover-induced homocitrate loss in nitrogenase; Nature Communications; Vol. 14; Art. No. 1091; PMCID PMC9968304; 10.1038/s41467-023-36636-4
• Threatt, Stephanie D. and Rees, Douglas C. (2023) Biological nitrogen fixation in theory, practice, and reality: a perspective on the molybdenum nitrogenase system; FEBS Letters; Vol. 597; No. 1; 45-58; PMCID PMC10100503; 10.1002/1873-3468.14534
• MacArdle, Siobhán G. and Rees, Douglas C. (2022) Solvent Deuterium Isotope Effects of Substrate Reduction by Nitrogenase from Azotobacter vinelandii; Journal of the American Chemical Society; Vol. 144; No. 46; 21125-21135; 10.1021/jacs.2c07574
• Miller, Ryan D. and Iinishi, Akira, el al. (2022) Computational identification of a systemic antibiotic for Gram-negative bacteria; Nature Microbiology; Vol. 7; No. 10; 1661-1672; 10.1038/s41564-022-01227-4
• Buscagan, Trixia M. and Kaiser, Jens T., el al. (2022) Selenocyanate derived Se-incorporation into the nitrogenase Fe protein cluster; eLife; Vol. 11; Art. No. e79311; 10.7554/elife.79311
• Fan, Chengcheng and Rees, Douglas C. (2022) Glutathione binding to the plant AtAtm3 transporter and implications for the conformational coupling of ABC transporters; eLife; Vol. 11; Art. No. e76140; PMCID PMC9000953; 10.7554/eLife.76140
• Fan, Chengcheng and Rees, Douglas C. (2022) Modeling the stimulation by glutathione of the steady state kinetics of an adenosine triphosphate binding cassette transporter; Protein Science; Vol. 31; No. 3; 752-757; PMCID PMC8862428; 10.1002/pro.4250
• Nichols, Aaron L. and Blumenfeld, Zack, el al. (2022) Fluorescence activation mechanism and imaging of drug permeation with new sensors for smoking-cessation ligands; eLife; Vol. 11; Art. No. e74648; PMCID PMC8820738; 10.7554/eLife.74648
• Kuznetsova, Anastasiya and Masrati, Gal, el al. (2021) Titratable transmembrane residues and a hydrophobic plug are essential for manganese import via the Bacillus anthracis ABC transporter MntBC-A; Journal of Biological Chemistry; Vol. 297; No. 4; Art. No. 101087; 10.1016/j.jbc.2021.101087
• Sharaf, Naima G. and Shahgholi, Mona, el al. (2021) Characterization of the ABC methionine transporter from Neisseria meningitidis reveals that lipidated MetQ is required for interaction; eLife; Vol. 10; Art. No. e69742; PMCID PMC8416018; 10.7554/eLife.69742
• Lee, Heui Beom and Shiau, Angela A., el al. (2021) CaMn₃^(IV)O₄ Cubane Models of the Oxygen Evolving Complex: Spin Ground States S < 9/2 and the Effect of Oxo Protonation; Angewandte Chemie International Edition; Vol. 60; No. 32; 17671-17679; PMCID PMC8319083; 10.1002/anie.202105303
• Probst, Corinna and Yang, Jing, el al. (2021) Mechanism of molybdate insertion into pterin-based molybdenum cofactors; Nature Chemistry; Vol. 13; No. 8; 758-765; PMCID PMC8325642; 10.1038/s41557-021-00714-1
• Buscagan, Trixia M. and Perez, Kathryn A., el al. (2021) Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site; Angewandte Chemie International Edition; Vol. 60; No. 11; 5704-5707; PMCID PMC7920927; 10.1002/anie.202015751
• Cho, Hye Jin and Kim, Kyung-su, el al. (2021) Microcrystal Electron Diffraction Elucidates Water-Specific Polymorphism-Induced Emission Enhancement of Bis-arylacylhydrazone; ACS Applied Materials & Interfaces; Vol. 13; No. 6; 7546-7555; 10.1021/acsami.0c21248
• Fan, Chengcheng and Rees, Douglas C. (2020) Crystal structure of the Escherichia coli transcription termination factor Rho; Acta Crystallographica Section F: Structural Biology and Crystallization Communications; Vol. 76; No. 9; Art. No. F76; PMCID PMC7470046; 10.1107/s2053230x20010572
• Fan, Chengcheng and Kaiser, Jens T., el al. (2020) A structural framework for unidirectional transport by a bacterial ABC exporter; Proceedings of the National Academy of Sciences of the United States of America; Vol. 117; No. 32; 19228-19236; PMCID PMC7430982; 10.1073/pnas.2006526117
• Einsle, Oliver and Rees, Douglas C. (2020) Structural Enzymology of Nitrogenase Enzymes; Chemical Reviews; Vol. 120; No. 12; 4969-5004; PMCID PMC8606229; 10.1021/acs.chemrev.0c00067
• Buscagan, Trixia M. and Rees, Douglas C. (2019) Rethinking the Nitrogenase Mechanism: Activating the Active Site; Joule; Vol. 3; No. 11; 2662-2678; PMCID PMC7451245; 10.1016/j.joule.2019.09.004
• Nguyen, Phong T. and Lai, Jeffrey Y., el al. (2019) Structures of the Neisseria meningitides methionine‐binding protein MetQ in substrate-free form and bound to L- and D-methionine isomers; Protein Science; Vol. 28; No. 10; 1750-1757; PMCID PMC6739813; 10.1002/pro.3694
• Henthorn, Justin T. and Arias, Renee J., el al. (2019) Localized Electronic Structure of Nitrogenase FeMoco Revealed by Selenium K-edge High Resolution X-ray Absorption Spectroscopy; Journal of the American Chemical Society; Vol. 141; No. 34; 13676-13688; PMCID PMC6716209; 10.1021/jacs.9b06988
• Wenke, Belinda B. and Spatzal, Thomas, el al. (2019) Site-specific oxidation state assignments of the irons in the [4Fe:4S]^(2+/1+/0) states of the nitrogenase Fe-protein; Angewandte Chemie International Edition; Vol. 58; No. 12; 3894-3897; PMCID PMC6519357; 10.1002/anie.201813966
• Fisher, Aaron J. and Mendoza-Denton, Rodolfo, el al. (2019) Structure and belonging: Pathways to success for underrepresented minority and women PhD students in STEM fields; PLoS ONE; Vol. 14; No. 1; Art. No. e0209279; PMCID PMC6326412; 10.1371/journal.pone.0209279
• Nguyen, Phong T. and Lai, Jeffrey Y., el al. (2018) Noncanonical role for the binding protein in substrate uptake by the MetNI methionine ATP Binding Cassette (ABC) transporter; Proceedings of the National Academy of Sciences of the United States of America; Vol. 115; No. 45; E10596-E10604; PMCID PMC6233128; 10.1073/pnas.1811003115
• Herrera, Nadia and Maksaev, Grigory, el al. (2018) Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance; Scientific Reports; Vol. 8; Art. No. 14566; PMCID PMC6167328; 10.1038/s41598-018-32536-6
• Arias, Renee J. and Kaiser, Jens T., el al. (2018) The "speed limit" for macromolecular crystal growth; Protein Science; Vol. 27; No. 10; 1837-1841; PMCID PMC6222248; 10.1002/pro.3491
• Segal, Helen M. and Spatzal, Thomas, el al. (2017) Electrochemical and Structural Characterization of Azotobacter vinelandii Flavodoxin II; Protein Science; Vol. 26; No. 10; 1984-1993; PMCID PMC5606536; 10.1002/pro.3236
• Morrison, Christine N. and Spatzal, Thomas, el al. (2017) Reversible Protonated Resting State of the Nitrogenase Active Site; Journal of the American Chemical Society; Vol. 139; No. 31; 10856-10862; PMCID PMC5553094; 10.1021/jacs.7b05695
• Zhang, Limei and Rees, Douglas C. (2017) Site-specific X-ray Absorption Spectroscopy Study on Nitrogenase MoFe-protein; Journal of Biological Inorganic Chemistry; Vol. 22; No. S1; S133; 10.1007/s00775-017-1475-y
• Bavi, Navid and Cortes, D. Marien, el al. (2016) The role of MscL amphipathic N terminus indicates a blueprint for bilayer-mediated gating of mechanosensitive channels; Nature Communications; Vol. 7; Art. No. 11984; PMCID PMC4917966; 10.1038/ncomms11984
• Spatzal, Thomas and Schlesier, Julia, el al. (2016) Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement; Nature Communications; Vol. 7; Art. No. 10902; PMCID PMC4793075; 10.1038/ncomms10902
• Yang, Janet G. and Rees, Douglas C. (2016) The Allosteric Regulatory Mechanism of the E.Coli Metni Methionine ABC Transporter; Biophysical Journal; Vol. 110; No. 3; 140A; 10.1016/j.bpj.2015.11.796
• Spatzal, Thomas and Perez, Kathryn A., el al. (2015) Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor; eLife; Vol. 4; Art. No. e11620; PMCID PMC4755756; 10.7554/eLife.11620
• Nguyen, Phong T. and Li, Qi Wen, el al. (2015) The contribution of methionine to the stability of the Escherichia coli MetNIQ ABC transporter-substrate binding protein complex; Biological Chemistry; Vol. 396; No. 9-10; 1127-1134; PMCID PMC4621241; 10.1515/hsz-2015-0131
• Mattle, Daniel and Zhang, Limei, el al. (2015) A sulfur-based transport pathway in Cu^+-ATPases; EMBO Reports; Vol. 16; No. 6; 728-740; PMCID PMC4467857; 10.15252/embr.201439927
• Walton, Troy A. and Idigo, Chinenye A., el al. (2015) MscL: channeling membrane tension; Pflügers Archiv European Journal of Physiology; Vol. 467; No. 1; 15-25; PMCID PMC4246047; 10.1007/s00424-014-1535-x
• Reading, Eamonn and Walton, Troy A., el al. (2015) The Effect of Detergent, Temperature, and Lipid on the Oligomeric State of MscL Constructs: Insights from Mass Spectrometry; Chemistry and Biology; Vol. 22; No. 5; 593-603; PMCID PMC6585436; 10.1016/j.chembiol.2015.04.016
• Yang, Janet G. and Rees, Douglas C. (2015) The Allosteric Regulatory Mechanism of the Escherichia coli MetNI Methionine ATP Binding Cassette (ABC) Transporter; Journal of Biological Chemistry; Vol. 290; No. 14; 9135-9140; PMCID PMC4423698; 10.1074/jbc.M114.603365
• Morrison, Christine N. and Hoy, Julie A., el al. (2015) Substrate Pathways in the Nitrogenase MoFe Protein by Experimental Identification of Small Molecule Binding Sites; Biochemistry; Vol. 54; No. 11; 2052-2060; PMCID PMC4590346; 10.1021/bi501313k
• Rees, Douglas C. (2015) Cotton Medal to Douglas Rees; Chemical and Engineering News; Vol. 93; No. 10; 49
• Rees, Douglas C. (2015) Powering brain power: GLUT1 and the era of structure based human transporter biology; National Science Review; Vol. 2; No. 1; 3-4; PMCID PMC4411962; 10.1093/nsr/nwu075
• Zhang, Li-Mei and Morrison, Christine N., el al. (2015) Nitrogenase MoFe protein from Clostridium pasteurianum at 1.08 Å resolution: comparison with the Azotobacter vinelandii MoFe protein; Acta Crystallographica Section D: Biological Crystallography; Vol. 71; No. 2; 274-282; PMCID PMC4321486; 10.1107/S1399004714025243
• Tezcan, F. Akif and Kaiser, Jens T., el al. (2015) Structural Evidence for Asymmetrical Nucleotide Interactions in Nitrogenase; Journal of the American Chemical Society; Vol. 137; No. 1; 146-149; PMCID PMC4304452; 10.1021/ja511945e
• Wang, Kaituo and Sitsel, Oleg, el al. (2014) Structure and mechanism of Zn^(2+)- transporting P-type ATPases; Nature; Vol. 514; No. 7523; 518-522; PMCID PMC4259247; 10.1038/nature13618
• Kamajaya, Aron and Kaiser, Jens T., el al. (2014) The Structure of a Conserved Piezo Channel Domain Reveals a Topologically Distinct β Sandwich Fold; Structure; Vol. 22; No. 10; 1520-1527; PMCID PMC4192063; 10.1016/j.str.2014.08.009
• Spatzal, Thomas and Perez, Kathryn A., el al. (2014) Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase; Science; Vol. 345; No. 6204; 1620-1623; PMCID PMC4205161; 10.1126/science.1256679
• Rees, Douglas (2014) Structural and Mechanistic Diversity of ABC Transporters; Protein Science; Vol. 23; No. S1; 70; 10.1002/pro.2504
• Lee, Jonas and Yang, Janet, el al. (2014) Structural and functional characterization of a heavy metal detoxifying ABC transporter; FASEB Journal; Vol. 28; No. 1; Art. No. Suppl. 997.2
• Lee, Jonas Y. and Yang, Janet G., el al. (2014) Structural Basis for Heavy Metal Detoxification by an Atm1-Type ABC Exporter; Science; Vol. 343; No. 6175; 1133-1136; PMCID PMC4151877; 10.1126/science.1246489
• Zhang, L. and Rees, D. C. (2014) Shining Light on the Metal Sites in Nitrogenase MoFe-protein by X-ray Anomalous Diffraction; Journal of Biological Inorganic Chemistry; Vol. 19; No. S1; S84; 10.1007/s00775-014-1095-8
• Rees, Douglas C. (2014) Structural and Mechanistic Diversity of ABC Transporters; Biophysical Journal; Vol. 106; No. 2; 434A; 10.1016/j.bpj.2013.11.2443
• Yang, Kun-Yun and Haynes, Chad A., el al. (2014) Turnover-Dependent Inactivation of the Nitrogenase MoFe-Protein at High pH; Biochemistry; Vol. 53; No. 2; 333-343; PMCID PMC3932303; 10.1021/bi4014769
• Meloni, Gabriele and Zhang, Limei, el al. (2014) Transmembrane Type-2-like Cu^(2+) Site in the P_(1B-3)-type ATPase CopB: Implications for Metal Selectivity; ACS Chemical Biology; Vol. 9; No. 1; 116-121; PMCID PMC3947036; 10.1021/cb400603t
• Basta, Tamara and Wu, Hsin-Jui, el al. (2014) Self-assembled lipid and membrane protein polyhedral nanoparticles; Proceedings of the National Academy of Sciences of the United States of America; Vol. 111; No. 2; 670-674; PMCID PMC3896197; 10.1073/pnas.1321936111
• Walton, Troy A. and Rees, Douglas C. (2013) Structure and stability of the C-terminal helical bundle of the E. coli mechanosensitive channel of large conductance; Protein Science; Vol. 22; No. 11; 1592-1601; PMCID PMC3831674; 10.1002/pro.2360
• Wu, H.-J. and Basta, T., el al. (2013) Microfluidic device for super-fast evaluation of membrane protein nanoparticle formation; Micro and Nano Letters; Vol. 8; No. 10; 672-675; 10.1049/mnl.2013.0216
• Zhang, Limei and Kaiser, Jens T., el al. (2013) The Sixteenth Iron in the Nitrogenase MoFe Protein; Angewandte Chemie International Edition; Vol. 52; No. 40; 10529-10532; PMCID PMC3891402; 10.1002/anie.201303877
• Howard, James B. and Kechris, Katerina J., el al. (2013) Multiple Amino Acid Sequence Alignment Nitrogenase Component 1: Insights into Phylogenetics and Structure-Function Relationships; PLoS ONE; Vol. 8; No. 9; Art. No. e72751; PMCID PMC3760896; 10.1371/journal.pone.0072751
• Lai, Jeffrey Y. and Poon, Yan Shuen, el al. (2013) Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 Å and 4.1 Å resolutions; Protein Science; Vol. 22; No. 4; 502-509; PMCID PMC3610056; 10.1002/pro.2222
• Pieper, Ursula and Schlessinger, Avner, el al. (2013) Coordinating the impact of structural genomics on the human α-helical transmembrane proteome; Nature Structural & Molecular Biology; Vol. 20; No. 2; 135-138; PMCID PMC3645303; 10.1038/nsmb.2508
• Bobyr, Elena and Lassila, Jonathan K., el al. (2012) High-Resolution Analysis of Zn^2+ Coordination in the Alkaline Phosphatase Superfamily by EXAFS and X-ray Crystallography; Journal of Molecular Biology; Vol. 415; No. 1; 102-117; PMCID PMC3249517; 10.1016/j.jmb.2011.10.040
• Johnson, Eric and Nguyen, Phong T., el al. (2012) Inward facing conformations of the MetNI methionine ABC transporter: Implications for the mechanism of transinhibition; Protein Science; Vol. 21; No. 1; 84-96; PMCID PMC3323783; 10.1002/pro.765
• Spatzal, Thomas and Aksoyoglu, Müge, el al. (2011) Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor; Science; Vol. 334; No. 6058; 940-940; PMCID PMC3268367; 10.1126/science.1214025
• Tirado-Lee, Laidamarie and Lee, Allen, el al. (2011) Classification of a Haemophilus influenzae ABC Transporter HI1470/71 through Its Cognate Molybdate Periplasmic Binding Protein, MoIA; Structure; Vol. 19; No. 11; 1701-1710; PMCID PMC3258573; 10.1016/j.str.2011.10.004
• Haswell, Elizabeth S. and Phillips, Rob, el al. (2011) Mechanosensitive Channels: What Can They Do and How Do They Do It?; Structure; Vol. 19; No. 10; 1356-1369; PMCID PMC3203646; 10.1016/j.str.2011.09.005
• Gandhi, Chris S. and Walton, Troy A., el al. (2011) OCAM: A new tool for studying the oligomeric diversity of MscL channels; Protein Science; Vol. 20; No. 2; 313-326; PMCID PMC3048416; 10.1002/pro.562
• Kaiser, Jens T. and Hu, Yilin, el al. (2011) Structure of Precursor-Bound NifEN: A Nitrogenase FeMo Cofactor Maturase/Insertase; Science; Vol. 331; No. 6013; 91-94; PMCID PMC3138709; 10.1126/science.1196954
• Liu, Zhenfeng and Walton, Troy A., el al. (2010) A reported archaeal mechanosensitive channel is a structural homolog of MarR-like transcriptional regulators; Protein Science; Vol. 19; No. 4; 808-814; PMCID PMC2867020; 10.1002/pro.360
• Lewinson, Oded and Lee, Allen T., el al. (2010) A distinct mechanism for the ABC transporter BtuCD–BtuF revealed by the dynamics of complex formation; Nature Structural & Molecular Biology; Vol. 17; No. 3; 332-339; PMCID PMC2924745; 10.1038/nsmb.1770
• Liu, Zhenfeng and Gandhi, Chris S., el al. (2009) Structure of a tetrameric MscL in an expanded intermediate state; Nature; Vol. 461; No. 7260; 120-124; PMCID PMC2737600; 10.1038/nature08277
• Lewinson, Oded and Lee, Allen T., el al. (2009) A P-type ATPase importer that discriminates between essential and toxic transition metals; Proceedings of the National Academy of Sciences of the United States of America; Vol. 106; No. 12; 4677-4682; PMCID PMC2651836; 10.1073/pnas.0900666106
• Rees, Douglas C. and Johnson, Eric, el al. (2009) ABC transporters: the power to change; Nature Reviews. Molecular Cell Biology; Vol. 10; No. 3; 218-227; PMCID PMC2830722; 10.1038/nrm2646
• Rice, Adrian E. and Mendez, Michael J., el al. (2009) Investigation of the biophysical and cell biological properties of ferroportin, a multipass integral membrane protein iron exporter; Journal of Molecular Biology; Vol. 386; No. 3; 717-732; PMCID PMC2677177; 10.1016/j.jmb.2008.12.063
• Gandhi, Chris S. and Rees, Douglas C. (2008) Opening the Molecular Floodgates; Science; Vol. 321; No. 5893; 1166-1167; 10.1126/science.1162963
• von Heijne, Gunnar and Rees, Douglas (2008) Membranes: reading between the lines; Current Opinion in Structural Biology; Vol. 18; No. 4; 403-405; 10.1016/j.sbi.2008.06.003
• Kadaba, Neena S. and Kaiser, Jens T., el al. (2008) The High-Affinity E. coli Methionine ABC Transporter: Structure and Allosteric Regulation; Science; Vol. 321; No. 5886; 250-253; PMCID PMC2527972; 10.1126/science.1157987
• Lewinson, Oded and Lee, Allen T., el al. (2008) The Funnel Approach to the Precrystallization Production of Membrane Proteins; Journal of Molecular Biology; Vol. 377; No. 1; 62-73; PMCID PMC2362151; 10.1016/j.jmb.2007.12.059
• Einsle, Oliver and Andrade, Susana L. A., el al. (2007) Assignment of Individual Metal Redox States in a Metalloprotein by Crystallographic Refinement at Multiple X-ray Wavelengths; Journal of the American Chemical Society; Vol. 129; No. 8; 2210-2211; PMCID PMC2527600; 10.1021/ja067562o
• Pinkett, H. W. and Lee, A. T., el al. (2007) An Inward-Facing Conformation of a Putative Metal-Chelate–Type ABC Transporter; Science; Vol. 315; No. 5810; 373-377; 10.1126/science.1133488
• Howard, James B. and Rees, Douglas C. (2006) How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation; Proceedings of the National Academy of Sciences of the United States of America; Vol. 103; No. 46; 17088-17093; PMCID PMC1859894; 10.1073/pnas.0603978103
• Borths, Elizabeth L. and Poolman, Bert, el al. (2005) In Vitro Functional Characterization of BtuCD-F, the Escherichia coli ABC Transporter for Vitamin B_(12) Uptake; Biochemistry; Vol. 44; No. 49; 16301-16309; 10.1021/bi0513103
• Tezcan, F. Akif and Kaiser, Jens T., el al. (2005) Nitrogenase Complexes: Multiple Docking Sites for a Nucleotide Switch Protein; Science; Vol. 309; No. 5739; 1377-1380; 10.1126/science.1115653
• Rees, Douglas C. and Tezcan, F. Akif, el al. (2005) Structural basis of biological nitrogen fixation; Philosophical Transactions A: Mathematical, Physical and Engineering Sciences; Vol. 363; No. 1829; 971-984; 10.1098/rsta.2004.1539
• Andrade, Susana L. A. and Cruz, Francisco, el al. (2005) Structures of the Iron-Sulfur Flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidus; Journal of Bacteriology; Vol. 187; No. 11; 3848-3854; 10.1128/JB.187.11.3848-3854.2005
• Corbett, Mary C. and Tezcan, F. Akif, el al. (2005) Mo K- and L-edge X-ray absorption spectroscopic study of the ADP·AlF_4^−-stabilized nitrogenase complex: comparison with MoFe protein in solution and single crystal; Journal of Synchrotron Radiation; Vol. 12; No. 1; 28-34; 10.1107/S0909049504027827
• Becker, Christian F. W. and Strop, Pavel, el al. (2004) Conversion of a Mechanosensitive Channel Protein from a Membrane-Embedded to a Water-Soluble form by Covalent Modification with Amphiphiles; Journal of Molecular Biology; Vol. 343; No. 3; 747-758; 10.1016/j.jmb.2004.08.062
• Nikolic-Hughes, Ivana and Rees, Douglas C., el al. (2004) Do Electrostatic Interactions with Positively Charged Active Site Groups Tighten the Transition State for Enzymatic Phosphoryl Transfer?; Journal of the American Chemical Society; Vol. 126; No. 38; 11814-11819; 10.1021/ja0480421
• Ambroggio, Xavier I. and Rees, Douglas C., el al. (2004) JAMM: A Metalloprotease-Like Zinc Site in the Proteasome and Signalosome; PLoS Biology; Vol. 2; No. 1; 113-119; PMCID PMC300881; 10.1371/journal.pbio.0020002
• Bass, Randal B. and Locher, Kaspar P., el al. (2003) The Structures of BtuCD and MscS and their Implications for Transporter and Channel Function; FEBS Letters; Vol. 555; No. 1; 111-115; 10.1016/S0014-5793(03)01126-8
• Locher, Kaspar P. and Bass, Randal B., el al. (2003) Breaching the Barrier; Science; Vol. 301; No. 5633; 603-604; 10.1126/science.1088621
• Perozo, Eduardo and Rees, Douglas C. (2003) Structure and Mechanism in Prokaryotic Mechanosensitive Channels; Current Opinion in Structural Biology; Vol. 13; No. 4; 432-442; 10.1016/S0959-440X(03)00106-4
• Rees, Douglas C. and Howard, James B. (2003) The Interface Between the Biological and Inorganic Worlds: Iron-Sulfur Metalloclusters; Science; Vol. 300; No. 5621; 929-931; 10.1126/science.1083075
• Shapovalov, George and Bass, Randal, el al. (2003) Open-State Disulfide Crosslinking between Mycobacterium tuberculosis Mechanosensitive Channel Subunits; Biophysical Journal; Vol. 84; No. 4; 2357-2365; PMCID PMC1302802; 10.1016/S0006-3495(03)75041-3
• Schmid, Benedikt and Einsle, Oliver, el al. (2002) Biochemical and Structural Characterization of the Cross-linked Complex of Nitrogenase: Comparison to the ADP-AIF_4^--Stabilized Structure; Biochemistry; Vol. 41; No. 52; 15557-15565; 10.1021/bi026642b
• Borths, Elizabeth L. and Locher, Kaspar P., el al. (2002) The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter; Proceedings of the National Academy of Sciences of the United States of America; Vol. 99; No. 26; 16642-16647; PMCID PMC139197; 10.1073/pnas.262659699
• Bass, Randal B. and Strop, Pavel, el al. (2002) Crystal Structure of Escherichia coli MscS, a Voltage-Modulated and Mechanosensitive Channel; Science; Vol. 298; No. 5598; 1582-1587; 10.1126/science.1077945
• Yeh, Andrew P. and Ambroggio, Xavier I., el al. (2002) High Resolution Crystal Structures of the Wild Type and Cys-55 right-arrow Ser and Cys-59 right-arrow Ser Variants of the Thioredoxin-like [2Fe-2S] Ferredoxin from Aquifex aeolicus; Journal of Biological Chemistry; Vol. 277; No. 37; 34499-34507; 10.1074/jbc.M205096200
• Einsle, Oliver and Tezcan, F. Akif, el al. (2002) Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-Cofactor; Science; Vol. 297; No. 5587; 1696-1700; 10.1126/science.1073877
• Rees, Douglas C. (2002) Great metalloclusters in enzymology; Annual Review of Biochemistry; Vol. 71; 221-246; 10.1146/annurev.biochem.71.110601.135406
• Spencer, Robert H. and Rees, ­Douglas C. (2002) The alpha-helix and the organization and gating of channels; Annual Review of Biophysics and Biomolecular Structure; Vol. 31; 207-233; 10.1146/annurev.biophys.31.082901.134329
• Axelrod, Herbert L. and Abresch, Edward C., el al. (2002) X-ray Structure Determination of the Cytochrome c_2: Reaction Center Electron Transfer Complex from Rhodobacter sphaeroides; Journal of Molecular Biology; Vol. 319; No. 2; 501-515; 10.1016/S0022-2836(02)00168-7
• Locher, Kaspar P. and Lee, Allen T., el al. (2002) The E. coli BtuCD Structure: A Framework for ABC Transporter Architecture and Mechanism; Science; Vol. 296; No. 5570; 1091-1098; 10.1126/science.1071142
• Iverson, Tina M. and Luna-Chavez, César, el al. (2002) Crystallographic studies of the Escherichia coli quinol-fumarate reductase with inhibitors bound to the quinol-binding site; Journal of Biological Chemistry; Vol. 277; No. 18; 16124-16130; 10.1074/jbc.M200815200
• Schmid, Benedikt and Ribbe, Markus W., el al. (2002) Structure of a Cofactor-Deficient Nitrogenase MoFe Protein; Science; Vol. 296; No. 5566; 352-356; 10.1126/science.1070010
• Rees, Douglas C. and Robertson, Andrew D. (2001) Some Thermodynamic Implications for the Thermostability of Proteins; Protein Science; Vol. 10; No. 6; 1187-1194; PMCID PMC2374017; 10.1110/ps.180101
• Chiu, Hsiu-Ju and Johnson, Eric, el al. (2001) Crystal Structures of a Novel Ferric Reductase from the Hyperthermophilic Archaeon Archaeoglobus fulgidus and Its Complex with NADP+; Structure; Vol. 9; No. 4; 311-319; 10.1016/S0969-2126(01)00589-5
• Iverson, Tina M. and Arciero, David M., el al. (2001) High-Resolution Structures of the Oxidized and Reduced States of Cytochrome c554 from Nitrosomonas europaea; Journal of Biological Inorganic Chemistry; Vol. 6; No. 4; 390-397; 10.1007/s007750100213
• Strop, Pavel and Smith, Kerry S., el al. (2001) Crystal Structure of the "cab"-type β Class Carbonic Anhydrase from the Archaeon Methanobacterium thermoautotrophicum; Journal of Biological Chemistry; Vol. 276; No. 13; 10299-10305; 10.1074/jbc.M009182200
• Locher, Kaspar P. and Hans, Marcus, el al. (2001) Crystal Structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA Dehydratase Component A; Journal of Molecular Biology; Vol. 307; No. 1; 297-308; 10.1006/jmbi.2000.4496
• Strop, Pavel and Takahara, Patricia M., el al. (2001) Crystal Structure of the All-ferrous [4Fe-4S]^0 Form of the Nitrogenase Iron Protein from Azotobacter vinelandii; Biochemistry; Vol. 40; No. 3; 651-656; 10.1021/bi0016467
• Chiu, Hsiu-Ju and Peters, John W., el al. (2000) MgATP-Bound and Nucleotide-Free Structures of a Nitrogenase Protein Complex between the Leu 127Δ-Fe-Protein and the MoFe-Protein; Biochemistry; Vol. 40; No. 3; 641-650; 10.1021/bi001645e
• Rees, Douglas C. and Howard, James B. (2000) Nitrogenase: Standing at the Crossroads; Current Opinion in Chemical Biology; Vol. 4; No. 5; 559-566; 10.1016/S1367-5931(00)00132-0
• Iverson, Tina M. and Alber, Birgit E., el al. (2000) A Closer Look at the Active Site of γ-Class Carbonic Anhydrases: High-Resolution Crystallographic Studies of the Carbonic Anhydrase from Methanosarcina thermophila; Biochemistry; Vol. 39; No. 31; 9222-9231; 10.1021/bi000204s
• Iverson, Tina M. and Luna-Chavez, César, el al. (2000) Analyzing Your Complexes: Structure of the Quinol-Fumarate Reductase Respiratory Complex; Current Opinion in Structural Biology; Vol. 10; No. 4; 448-455; 10.1016/S0959-440X(00)00113-5
• Yeh, Andrew P. and Chatelet, Claire, el al. (2000) Structure of a Thioredoxin-like [2Fe-2S] Ferredoxin from Aquifex aeolicus; Journal of Molecular Biology; Vol. 300; No. 3; 587-595; 10.1006/jmbi.2000.3871
• Yeh, Andrew P. and Hu, Yonglin, el al. (2000) Structures of the Superoxide Reductase from Pyrococcus furiosus in the Oxidized and Reduced States; Biochemistry; Vol. 39; No. 10; 2499-2508; 10.1021/bi992428k
• Kielkopf, Clara L. and Ding, Sheng, el al. (2000) Conformational Flexibility of B-DNA at 0.74 Å Resolution: d(CCAGTACTGG)_2; Journal of Molecular Biology; Vol. 296; No. 3; 787-801; 10.1006/jmbi.1999.3478
• Kielkopf, Clara L. and Erkkila, Kathryn E., el al. (2000) Structure of a photoactive rhodium complex intercalated into DNA; Nature Structural Biology; Vol. 7; No. 2; 117-121; 10.1038/72385
• Kielkopf, Clara L. and Bremer, Ryan M., el al. (2000) Structural Effects of DNA Sequence on T•A Recognition by Hydroxypyrrole/Pyrrole Pairs in the Minor Groove; Journal of Molecular Biology; Vol. 295; No. 3; 557-567; 10.1006/jmbi.1999.3364
• Rees, Douglas C. and Chang, Geoffrey, el al. (2000) Crystallographic Analyses of Ion Channels: Lessons and Challenges; Journal of Biological Chemistry; Vol. 275; No. 2; 713-716
• Rees, Douglas C. and Howard, James B. (1999) Structural Bioenergetics and Energy Transduction Mechanisms; Journal of Molecular Biology; Vol. 293; No. 2; 343-350; 10.1006/jmbi.1999.3005
• Spencer, Robert H. and Chang, Geoffrey, el al. (1999) Feeling the Pressure: Structural Insights into a Gated Mechanosensitive Channel; Current Opinion in Structural Biology; Vol. 9; No. 4; 448-454; 10.1016/S0959-440X(99)80063-3
• Iverson, Tina M. and Luna-Chavez, César, el al. (1999) Structure of the Escherichia coli Fumarate Reductase Respiratory Complex; Science; Vol. 284; No. 5422; 1961-1966; 10.1126/science.284.5422.1961
• Grossmann, J. Günter and Hasnain, S. Samar, el al. (1999) Comparing Crystallographic and Solution Structures of Nitrogenase Complexes; Acta Crystallographica Section D: Biological Crystallography; Vol. 55; No. 4; 727-728; 10.1107/S0907444999003856
• Hu, Yonglin and Faham, Salem, el al. (1999) Formaldehyde Ferredoxin Oxidoreductase from Pyrococcus furiosus: The 1.85 Å Resolution Crystal Structure and its Mechanistic Implications; Journal of Molecular Biology; Vol. 286; No. 3; 899-914; 10.1006/jmbi.1998.2488
• Faham, Salem and Day, Michael W., el al. (1999) Structures of Ruthenium-modified Pseudomonas aeruginosa Azurin and [Ru(2,2'-bipyridine)_2(imidazole)_2)]SO_4•10H_2O; Acta Crystallographica Section D: Biological Crystallography; Vol. 55; No. 2; 379-385; 10.1107/S0907444998010464
• Chang, Geoffrey and Spencer, Robert H., el al. (1998) Structure of the MscL Homolog from Mycobacterium tuberculosis: A Gated Mechanosensitive Ion Channel; Science; Vol. 282; No. 5397; 2220-2226; 10.1126/science.282.5397.2220
• Iverson, Tina M. and Arciero, David M., el al. (1998) Heme Packing Motifs Revealed by the Crystal Structure of the Tetra-heme Cytochrome c554 from Nitrosomonas europaea; Nature Structural Biology; Vol. 5; No. 11; 1005-1012; 10.1038/2975
• Kielkopf, Clara L. and White, Sarah, el al. (1998) A Structural Basis for Recognition of A·T and T·A Base Pairs in the Minor Groove of B-DNA; Science; Vol. 282; No. 5386; 111-115; 10.1126/science.282.5386.111
• Faham, Salem and Linhardt, Robert J., el al. (1998) Diversity Does Make a Difference: Fibroblast Growth Factor-Heparin Interactions; Current Opinion in Structural Biology; Vol. 8; No. 5; 578-586; 10.1016/S0959-440X(98)80147-4
• Bau, Robert and Rees, Douglas C., el al. (1998) Crystal structure of rubredoxin from Pyrococcus furiosus at 0.95 Å resolution, and the structures of N-terminal methionine and formylmethionine variants of Pf Rd. Contributions of N-terminal interactions to thermostability; Journal of Biological Inorganic Chemistry; Vol. 3; No. 5; 484-493; 10.1007/s007750050258
• Schlessman, James L. and Woo, Deborah, el al. (1998) Conformational Variability in Structures of the Nitrogenase Iron Proteins from Azotobacter vinelandii and Clostridium pasteurianum; Journal of Molecular Biology; Vol. 280; No. 4; 669-685; 10.1006/jmbi.1998.1898
• Kielkopf, Clara L. and Baird, Eldon E., el al. (1998) Structural Basis for G•C Recognition in the DNA Minor Groove; Nature Structural Biology; Vol. 5; No. 2; 104-109; 10.1038/nsb0298-104
• Rees, Douglas C. and Hu, Yonglin, el al. (1997) A crystallographic view of the molybdenum cofactor; Journal of the Chemical Society. Dalton Transactions; Vol. 1997; No. 21; 3909-3914; 10.1039/a704048b
• Magnuson, Jon K. and Paustian, Timothy D., el al. (1997) Nitrogenase Iron-Molybdenum Cofactor Binding Site: Protein Conformational Changes Associated with Cofactor Binding; Tetrahedron; Vol. 53; No. 35; 11971-11984; 10.1016/S0040-4020(97)00710-2
• Hu, Yonglin and Rech, Sabina, el al. (1997) Crystal Structure of the Molybdate Binding Protein ModA; Nature Structural Biology; Vol. 4; No. 9; 703-707; 10.1038/nsb0997-703
• Faham, Salem and Mizoguchi, Tadashi J., el al. (1997) Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the Cu^(II(Cys112Asp) protein; Journal of Biological Inorganic Chemistry; Vol. 2; No. 4; 464-469; 10.1007/s007750050157
• Kisker, Caroline and Schindelin, Hermann, el al. (1997) Molybdenum-cofactor-containing enzymes: structure and mechanism; Annual Review of Biochemistry; Vol. 66; 233-267; 10.1146/annurev.biochem.66.1.233
• Schindelin, Hermann and Kisker, Caroline, el al. (1997) The Structure of the ADP•AlF4- stabilized nitrogenase complex and its implications for signal transduction mechanism; Nature; Vol. 387; 370-376; 10.1038/387370a0
• Schindelin, Hermann and Kisker, Caroline, el al. (1997) Structure of ADP·AIF_4 -stabilized nitrogenase complex and its implications for signal transduction; Nature; Vol. 387; No. 6631; 370-376; 10.1038/387370a0
• Stowell, M. H. B. and McPhillips, T. M., el al. (1997) Light-Induced Structural Changes in Photosynthetic Reaction Center: Implications for Mechanism of Electron-Proton Transfer; Science; Vol. 276; No. 5313; 812-816; 10.1126/science.276.5313.812
• Soltis, S. Michael and Stowell, Michael H. B., el al. (1997) Successful Flash-Cooling of Xenon Derivatized Myoglobin Crystals; Journal of Applied Crystallography; Vol. 30; No. 2; 190-194; 10.1107/S0021889896012939
• Peters, John W. and Stowell, Michael H. B., el al. (1997) Redox-Dependent Structural Changes in the Nitrogenase P-Cluster; Biochemistry; Vol. 36; No. 6; 1181-1187; 10.1021/bi9626665
• Peters, John W. and Stowell, Michael H. B., el al. (1996) A leucine-rich repeat variant with a novel repetitive protein structural motif; Nature Structural Biology; Vol. 3; No. 12; 991-994; 10.1038/nsb1296-991
• Johnson, Michael K. and Rees, Douglas C., el al. (1996) Tungstoenzymes; Chemical Reviews; Vol. 96; No. 7; 2817-2840; 10.1021/cr950063d
• Howard, James B. and Rees, Douglas C. (1996) Structural Basis of Biological Nitrogen Fixation; Chemical Reviews; Vol. 96; No. 7; 2965-2982; 10.1021/cr9500545
• Stowell, Michael H. B. and Soltis, S. Michael, el al. (1996) A simple device for studying macromolecular crystals under moderate gas pressures (0.1-10 MPa); Journal of Applied Crystallography; Vol. 29; No. 5; 608-613; 10.1107/S0021889896004712
• Schindelin, Hermann and Kisker, Caroline, el al. (1996) Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination; Science; Vol. 272; No. 5268; 1615-1621; 10.1126/science.272.5268.1615
• Kisker, Caroline and Schindelin, Hermann, el al. (1996) A Left-handed β Helix Revealed by the Crystal Structure of a Carbonic Anhydrase from the Archaeon Methanosarcina thermophila; EMBO Journal; Vol. 15; No. 10; 2323-2330; PMCID PMC450161
• McPhillips, Timothy M. and Hsu, Barbara T., el al. (1996) Structure of the R65Q Mutant of Yeast 3-Phosphoglycerate Kinase Complexed with Mg-AMP-PNP and 3-Phospho-d-glycerate; Biochemistry; Vol. 35; No. 13; 4118-4127; 10.1021/bi952500o
• Faham, S. and Hileman, R. E., el al. (1996) Heparin Structure and Interactions with Basic Fibroblast Growth Factor; Science; Vol. 271; No. 5252; 1116-1120; 10.1126/science.271.5252.1116
• Stowell, Michael H. B. and Rock, Ronald S., el al. (1996) Efficient Synthesis of Photolabile Alkoxy Benzoin Protecting Groups; Tetrahedron Letters; Vol. 37; No. 3; 307-310; 10.1016/0040-4039(95)02159-0
• Joshua-Tor, Leemor and Xu, H. Eric, el al. (1995) Crystal structure of a conserved protease that binds DNA: the bleomycin hydrolase, Gal6; Science; Vol. 269; No. 5226; 945-950; 10.1126/science.7638617
• Kletzin, Arnulf and Mukund, Swarnalatha, el al. (1995) Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis; Journal of Bacteriology; Vol. 177; No. 16; 4817-4819; PMCID PMC177251
• Arakawa, Tsutomu and Holst, Paige, el al. (1995) The importance of Arg40 and 45 in the mitogenic activity and structural stability of basic fibroblast growth factor: Effects of acidic amino acid substitutions; Journal of Protein Chemistry; Vol. 14; No. 5; 263-274; 10.1007/BF01886783
• Rees, Douglas C. and Adams, Michael W. W. (1995) Hyperthermophiles: Taking the Heat and Loving It; Structure; Vol. 3; No. 3; 251-254; 10.1016/S0969-2126(01)00155-1
• Chan, Michael K. and Mukund, Swarnalatha, el al. (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase; Science; Vol. 267; No. 5203; 1463-1469; 10.1126/science.7878465
• Stowell, Michael H. B. and Rees, Douglas C. (1995) Structure and Stability of Membrane Proteins; Advances in Protein Chemistry; Vol. 46; 279-311; 10.1016/S0065-3233(08)60338-1
• Howard, James B. and Rees, Douglas C. (1994) Nitrogenase: A nucleotide-dependent molecular switch; Annual Review of Biochemistry; Vol. 63; 235-264; 10.1146/annurev.bi.63.070194.001315
• Axelrod, Herbert L. and Feher, George, el al. (1994) Crystallization and X-ray Structure Determination of Cytochrome c_2 from Rhodobacter sphaeroides in Three Crystal Forms; Acta Crystallographica Section D: Biological Crystallography; Vol. 50; No. 4; 596-602; 10.1107/S0907444994001319
• Chirino, Arthur J. and Lous, Erik J., el al. (1994) Crystallographic Analyses of Site-Directed Mutants of the Photosynthetic Reaction Center from Rhodobacter sphaeroides; Biochemistry; Vol. 33; No. 15; 4584-4593; 10.1021/bi00181a020
• Kim, Jongsun and Rees, Douglas C. (1994) Nitrogenase and Biological Nitrogen Fixation; Biochemistry; Vol. 33; No. 2; 389-397; 10.1021/bi00168a001
• Rees, Douglas C. (1993) Dinitrogen Reduction by Nitrogenase: If N_2 Isn't Broken, It Can't be Fixed; Current Opinion in Structural Biology; Vol. 3; No. 6; 921-928; 10.1016/0959-440X(93)90157-G
• Kim, Kyoung-Hee and Kwon, Byoung-Mog, el al. (1993) Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex; Science; Vol. 262; No. 5136; 1042-1046; 10.1126/science.8235619
• Rees, Douglas C. and Wolfe, Gershon M. (1993) Macromolecular Solvation Energies Derived from Small Molecule Crystal Morphology; Protein Science; Vol. 2; No. 11; 1882-1889; PMCID PMC2142285; 10.1002/pro.5560021110
• Zhu, Xiaotian and Hsu, Barbara T., el al. (1993) Structural studies of the binding of the anti-ulcer drug sucrose octasulfate to acidic fibroblast growth factor; Structure; Vol. 1; No. 1; 27-34; 10.1016/0969-2126(93)90006-3
• Kim, Jongsun and Woo, D., el al. (1993) X-ray Crystal Structure of the Nitrogenase Molybdenum-Iron Protein from Clostridium pasteurianum at 3.0-Å Resolution; Biochemistry; Vol. 32; No. 28; 7104-7115; 10.1021/bi00079a006
• Arakawa, Tsutomu and Horan, Thomas P., el al. (1993) Production and Characterization of an Analog of Acidic Fibroblast Growth Factor with Enhanced Stability and Biological Activity; Protein Engineering; Vol. 6; No. 5; 541-546; 10.1093/protein/6.5.541
• Chan, Michael K. and Kim, Jongsun, el al. (1993) The Nitrogenase FeMo-Cofactor and P-Cluster Pair: 2.2 Å Resolution Structures; Science; Vol. 260; No. 5109; 792-794; 10.1126/science.8484118
• Stowell, Michael H. B. and Larsen, Randy W., el al. (1993) Transient electron-transfer studies on the two-subunit cytochrome c oxidase from Paracoccus denitrificans; Journal of Physical Chemistry; Vol. 97; No. 12; 3054-3057; 10.1021/j100114a036
• Rees, Douglas C. and Chan, Michael K., el al. (1993) Structure and Function of Nitrogenase; Advances in Inorganic Chemistry; Vol. 40; 89-119; 10.1016/S0898-8838(08)60182-8
• Kim, Jongsun and Rees, D. C. (1992) Crystallographic Structure and Functional Implications of the Nitrogenase Molybdenum-Iron Protein from Azotobacter vinelandii; Nature; Vol. 360; No. 6404; 553-560; 10.1038/360553a0
• Day, Michael W. and Hsu, Barbara T., el al. (1992) X-ray Crystal Structures of the Oxidized and Reduced forms of the Rubredoxin from the Marine Hyperthermophilic Archaebacterium Pyrococcus furiosus; Protein Science; Vol. 1; No. 11; 1494-1507; PMCID PMC2142115; 10.1002/pro.5560011111
• Blake, Paul R. and Day, Michael W., el al. (1992) Comparison of the X-ray Structure of Native Rubredoxin from Pyrococcus furiosus with the NMR Structure of the Zinc-Substituted Protein; Protein Science; Vol. 1; No. 11; 1522-1525; PMCID PMC2142123; 10.1002/pro.5560011113
• Kim, Jongsun and Rees, D. C. (1992) Structural models for the metal centers in the nitrogenase molybdenum-iron protein; Science; Vol. 257; No. 5077; 1677-1682; 10.1126/science.1529354
• Georgiadis, M. M. and Komiya, H., el al. (1992) Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii; Science; Vol. 257; No. 5077; 1653-1659; 10.1126/science.1529353
• Krantzman, Kristin D. and Rees, Douglas C., el al. (1991) Computational Study of the Imaging of a Molecular Crystal with the Atomic Force Microscope; Journal of Physical Chemistry; Vol. 95; No. 23; 9039-9042; 10.1021/j100176a006
• Zhu, X. and Komiya, H., el al. (1991) Three-Dimensional Structures of Acidic and Basic Fibroblast Growth Factors; Science; Vol. 251; No. 4989; 90-93; 10.1126/science.1702556
• Rees, Douglas C. (1990) An Envelope-based Approach for Direct Phase Determination of Macromolecular Structures; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 46; No. 11; 915-922; 10.1107/S0108767390006705
• Rees, D. C. and DeAntonio, L., el al. (1989) Hydrophobic organization of membrane proteins; Science; Vol. 245; No. 4917; 510-513; 10.1126/science.2667138
• Rees, D. C. and Komiya, H., el al. (1989) The Bacterial Photosynthetic Reaction Center as a Model for Membrane Proteins; Annual Review of Biochemistry; Vol. 58; 607-633; 10.1146/annurev.bi.58.070189.003135
• Willing, Andreas H. and Georgiadis, Millie M., el al. (1989) Cross-linking of Nitrogenase Components: Structure and Activity of the Covalent Complex; Journal of Biological Chemistry; Vol. 264; No. 15; 8499-8503
• Feher, G. and Allen, J. P., el al. (1989) Structure and Function of Bacterial Photosynthetic Reaction Centers; Nature; Vol. 339; No. 6220; 111-116; 10.1038/339111a0
• Komiya, H. and Yeates, T. O., el al. (1988) Structure of the Reaction Center from Rhodopseudomonas sphaeroides R-26 and 2.4.1: Symmetry Relations and Sequence Comparisons between Different Species; Proceedings of the National Academy of Sciences of the United States of America; Vol. 85; No. 23; 9012-9016; PMCID PMC282652
• Yeates, T. O. and Rees, D. C. (1988) Versatile Rigid-Body and Group Refinement in Real Space; Journal of Applied Crystallography; Vol. 21; No. 6; 925-928; 10.1107/S0021889888007927
• Yeates, T. O. and Komiya, H., el al. (1988) Structure of the Reaction Center from Rhodopseudomonas sphaeroides R-26 and 2.4.1: Protein-Cofactor (Bacteriochlorophyll, Bacteriopheophytin and Carotenoid) Interactions; Proceedings of the National Academy of Sciences of the United States of America; Vol. 85; No. 21; 7993-7997; PMCID PMC282340
• Allen, J. P. and Feher, G., el al. (1988) Structure of the Reaction Center from Rhodopseudomonas sphaeroides R-26: Protein-Cofactor (Quinones and Fe^(2+)) Interactions; Proceedings of the National Academy of Sciences of the United States of America; Vol. 85; No. 22; 8487-8491; PMCID PMC282483
• Allen, J. P. and Feher, G., el al. (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits; Proceedings of the National Academy of Sciences of the United States of America; Vol. 84; No. 17; 6162-6166; PMCID PMC299029
• Yeates, T. O. and Komiya, H., el al. (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions; Proceedings of the National Academy of Sciences of the United States of America; Vol. 84; No. 18; 6438-6442; PMCID PMC299092
• Allen, J. P. and Feher, G., el al. (1987) Structure of the Reaction Center from Rhodopseudomonas sphaeroides R-26: The Cofactors; Proceedings of the National Academy of Sciences of the United States of America; Vol. 84; No. 16; 5730-5734; PMCID PMC298936; 10.1073/pnas.84.16.5730
• Yeates, T. O. and Rees, D. C. (1987) An Isomorphous Replacement Method for Phasing Twinned Structures; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 43; No. 1; 30-36; 10.1107/S0108767387099951
• Knossow, M. and Lewis, M., el al. (1986) The refinement of the haemagglutinin membrane glycoprotein of influenza virus; Acta crystallographica. Section B, Structural science; Vol. 42; No. 6; 627-632; 10.1107/S0108768186097628
• Allen, J. P. and Feher, G., el al. (1986) Structural Homology of Reaction Centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as Determined by X-ray Diffraction; Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 22; 8589-8593; PMCID PMC386976
• Chakrabarti, P. and Bernard, M., el al. (1986) Peptide Bond Distortion and the Curvature of α-helices; Biopolymers; Vol. 25; No. 6; 1087-1093; 10.1002/bip.360250609
• Lewis, Mitchell and Rees, D. C. (1985) Fractal Surfaces of Proteins; Science; Vol. 230; No. 4730; 1163-1165; 10.1126/science.4071040
• Rees, D. C. (1985) Electrostatic Influence on the Energetics of Electron Transfer Reactions; Proceedings of the National Academy of Sciences of the United States of America; Vol. 82; No. 10; 3082-3085; PMCID PMC397718; 10.1073/pnas.82.10.3082
• Dickerson, Joyce L. and Kornuc, John J., el al. (1985) Complex Formation between Flavodoxin and Cytochrome c: Cross-linking Studies; Journal of Biological Chemistry; Vol. 260; No. 8; 5175-5178
• Shoham, G. and Rees, D. C., el al. (1984) Effects of pH on the Structure and Function of Carboxypeptidase A: Crystallographic Studies; Proceedings of the National Academy of Sciences of the United States of America; Vol. 81; No. 24; 7767-7771; PMCID PMC392233
• Shoham, G. and Rees, D. C., el al. (1984) Crystal and Molecular Structure of S-Deoxo[Ile^3]amaninamide: A Synthetic Analog of Amanita Toxins; Journal of the American Chemical Society; Vol. 106; No. 16; 4606-4615; 10.1021/ja00328a051
• Rees, D. C. (1984) Systematic Distortion of Peptide Bond Angeles in Beta Sheets: Evidence for cis-trans Isomerization?; Transactions of the American Crystallographic Association; Vol. 20; 145-148
• Rees, D. C. (1984) A General Solution for the Steady-State Kinetics of Immobilized Enzyme Systems; Bulletin of Mathematical Biology; Vol. 46; No. 2; 229-234; 10.1007/BF02460071
• Rees, D. C. and Lipscomb, W. N. (1983) Crystallographic Studies on Apocarboxypeptidase A and the Complex with Glycyl-L-Tyrosine; Proceedings of the National Academy of Sciences of the United States of America; Vol. 80; No. 23; 7151-7154; PMCID PMC390011
• Rees, D. C. (1983) Largest Likely Values for R factors Calculated After Phase Refinement by Non-crystallographic Symmetry Averaging; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 39; No. 6; 916-920; 10.1107/S010876738300183X
• Rees, D. C. and Howard, James Bryant (1983) Crystallization of Azotobacter vinelandii Nitrogenase Iron Protein; Journal of Biological Chemistry; Vol. 258; No. 20; 12733-12734
• Rees, D. C. and Lewis, M., el al. (1983) Refined Crystal Structure of Carboxypeptidase A at 1.54Å Resolution; Journal of Molecular Biology; Vol. 168; No. 2; 367-387; 10.1016/S0022-2836(83)80024-2
• Lewis, Mitchell and Rees, D. C. (1983) Statistical Modification of Anomalous-Scattering Differences; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 39; No. 4; 512-515; 10.1107/S0108767383000999
• Rees, Douglas (1983) Biopower; Journal of Chemical Education; Vol. 60; No. 4; 289; 10.1021/ed060p289
• Rees, D. C. and Lewis, Mitchell (1983) Incorporation of Experimental Phases in a Restrained Least-Squares Refinement; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 39; No. 1; 94-97; 10.1107/S0108767383000173
• Rees, D. C. and Lipscomb, W. N. (1982) Refined Crystal Structure of the Potato Inhibitor Complex of Carboxypeptidase A at 2.5 Å Resolution; Journal of Molecular Biology; Vol. 160; No. 3; 475-498; 10.1016/0022-2836(82)90309-6
• Rees, D. C. (1982) A General Theory of X-ray Intensity Statistics for Twins by Merohedry; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 38; No. 2; 201-207; 10.1107/S056773948200045X
• Rees, D. C. and Lipscomb, W. N. (1981) Binding of Ligands to the Active Site of Carboxypeptidase A; Proceedings of the National Academy of Sciences of the United States of America; Vol. 78; No. 9; 5455-5459; 10.1073/pnas.78.9.5455
• Rees, D. C. and Lewis, M., el al. (1981) Zinc Environment and cis Peptide Bonds in Carboxypeptidase A at 1.75Å Resolution; Proceedings of the National Academy of Sciences of the United States of America; Vol. 78; No. 6; 3408-3412; PMCID PMC319577
• Rees, Douglas C. (1980) Experimental Evaluation of the Effective Dielectric Constant of Proteins; Journal of Molecular Biology; Vol. 141; No. 3; 323-326; 10.1016/0022-2836(80)90184-9
• Rees, Douglas C. and Lipscomb, William N. (1980) Structure of the Potato Inhibitor Complex of Carboxypeptidase A at 2.5Å Resolution; Proceedings of the National Academy of Sciences of the United States of America; Vol. 77; No. 8; 4633-4637; PMCID PMC349899
• Rees, Douglas C. (1980) The Influence of Twinning by Merohedry on Intensity Statistics; Acta Crystallographica. Section A, Foundations of Crystallography; Vol. 36; No. 4; 578-581; 10.1107/S0567739480001234
• Rees, Douglas C. and Honzatko, Richard B., el al. (1980) The Structure of an Actively Exchanging Complex between Carboxypeptidase A and a Substrate Analogue; Proceedings of the National Academy of Sciences of the United States of America; Vol. 77; No. 6; 3288-3291; PMCID PMC349600
• Rees, Douglas C. and Lipscomb, William N. (1980) Structure of Potato Inhibitor Complex of Carboxypeptidase A at 5.5Å Resolution; Proceedings of the National Academy of Sciences of the United States of America; Vol. 77; No. 1; 277-280; PMCID PMC348252; 10.1073/pnas.77.1.277
• Chan, Shung Kai and Rees, Douglas C., el al. (1976) Linear Structure of the Oligosaccharide Chains in α_1-Protease Inhibitor Isolated from Human Plasma; Journal of Biological Chemistry; Vol. 251; No. 2; 471-476
• Chan, S. K. and Rees, D. C. (1975) Molecular Basis for the α_1-Protease Inhibitor Deficiency; Nature; Vol. 255; No. 5505; 240-241; 10.1038/255240a0
• Slayman, Carolyn W. and Rees, Douglas C., el al. (1975) Generation of Adenosine Triphosphate in Cytochrome-deficient Mutants of Neurospora; Journal of Biological Chemistry; Vol. 250; No. 2; 396-408
• Lester, Robert L. and Smith, Sharron W., el al. (1974) The Isolation and Partial Characterization of Two Novel Sphingolipids from Neurospora crassa: Di(Inositolphosphoryl)ceramide and [(gal)_3glu]ceramide; Journal of Biological Chemistry; Vol. 249; No. 11; 3388-3394