doi.bio/jane_s_richardson


Jane S. Richardson

Early Life and Education

Jane Shelby Richardson, born on January 25, 1941, in Teaneck, New Jersey, is an American biophysicist known for her work in biochemistry, molecular graphics, and protein structure representation. Richardson's parents encouraged her interest in science from a young age. She participated in local astronomy clubs and won third place in the Westinghouse Science Talent Search in 1958 by calculating the satellite Sputnik's orbit through her observations.

Richardson attended Teaneck High School and later enrolled at Swarthmore College, initially intending to study mathematics, astronomy, and physics. However, she graduated with a Bachelor of Arts in philosophy and a minor in physics in 1962. She then pursued graduate studies in philosophy at Harvard University, obtaining a Master of Arts and a Master of Arts in Teaching in 1966.

Career and Research

Richardson's career path took an unexpected turn when she joined her husband, David C. Richardson, at the Massachusetts Institute of Technology (MIT). There, she worked as a technician in the same laboratory where her husband was pursuing his doctorate using X-ray crystallography to study protein structures. This marked the beginning of their long-standing research collaboration.

The Richardsons moved to Duke University in 1970, where they jointly head a research group to this day. They are known for their pioneering work in protein crystallography and the development of the ribbon diagram, also known as the Richardson diagram, which illustrates the 3D structure of proteins. This diagram has become a standard representation, facilitating global investigations into protein structure and function.

In addition to their work on protein structure representation, the Richardsons have made significant contributions to synthetic biochemistry and computational biology. They were early pioneers in the de novo design of proteins, using a reverse engineering approach to understand protein folding. They also developed the kinemage system of molecular graphics and the Mage program to display 3D protein structures on computers.

Awards and Recognition

Jane Richardson has received numerous awards and recognition for her work. She was awarded a MacArthur Fellowship in 1985, also known as the "Genius Grant," and was elected to the National Academy of Sciences and the American Academy of Arts and Sciences in 1991. In 2006, she was elected to the National Academy of Medicine, and in 2012, she became a fellow of the American Crystallographic Association. Richardson served as president of the Biophysical Society for the 2012-2013 term.

Notable Publications

Current Position

Jane S. Richardson is currently a James B. Duke Professor of Biochemistry at Duke University, where she continues to run the Richardson Laboratory alongside her husband.

Jane S. Richardson

Biography

Jane Shelby Richardson (born 25 January 1941) is an American biophysicist and professor of biochemistry at Duke University. She is best known for developing the Richardson diagram, or ribbon diagram, a method of representing the 3D structure of proteins.

Early Life and Education

Richardson grew up in Teaneck, New Jersey, and attended Teaneck High School. Her parents encouraged her interest in science, and she was a member of local astronomy clubs from elementary school. In 1958, she won third place in the Westinghouse Science Talent Search, submitting calculations of the satellite Sputnik's orbit from her own observations.

Richardson attended Swarthmore College, intending to study mathematics, astronomy, and physics. However, she graduated with a bachelor's degree in philosophy and a minor in physics in 1962. She then pursued graduate studies in philosophy at Harvard University, obtaining a master's degree in 1966. After a brief stint teaching high school, Richardson returned to the scientific field, working as a technician at MIT alongside her husband, David Richardson, whom she met at Swarthmore.

Career

At MIT, Richardson gained technical skills and a scientific background in biochemistry and biophysics while working in her husband's laboratory. She began drawing diagrams to interpret protein molecule structures, developing the eponymous Richardson diagram or ribbon diagram. This method of illustrating protein structures has become a standard representation, facilitating global investigations of protein structure and function.

Richardson and her husband moved to Duke University in 1970, where they jointly head a research group. They are known for their pioneering work in protein crystallography, de novo protein design, and molecular graphics. They developed methods to calculate hydrogen-atom contacts, improving the accuracy of macromolecular structures.

Richardson has received numerous accolades for her contributions to science. In 1985, she was awarded a MacArthur Fellowship, also known as the "Genius Grant." She was elected to the National Academy of Sciences and the American Academy of Arts and Sciences in 1991 and to the Institute of Medicine in 2006. In 2012, she became a fellow of the American Crystallographic Association and served as president of the Biophysical Society for the 2012-2013 term. In 2019, she received the Alexander Hollaender Award in Biophysics.

Publications

Richardson's highly cited publications include:

Google Scholar Profile

Jane S Richardson)

Google Scholar

Jane S. Richardson Professor of Biochemistry, Duke University http://kinemage.biochem.duke.edu/ PHENIX: a comprehensive Python-based system for macromolecular structure solution PD Adams, PV Afonine, G Bunkóczi, VB Chen, IW Davis, N Echols, … Acta Crystallographica Section D: Biological Crystallography 66 (2), 213-221, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:qjMakFHDy7sC Cited by: 23685

MolProbity: all-atom structure validation for macromolecular crystallography VB Chen, WB Arendall, JJ Headd, DA Keedy, RM Immormino, GJ Kapral, … Acta Crystallographica Section D: Biological Crystallography 66 (1), 12-21, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Y0pCki6q_DkC Cited by: 14195

Structure validation by Cα geometry: ϕ, ψ and Cβ deviation SC Lovell, IW Davis, WB Arendall III, PIW De Bakker, JM Word, … Proteins: Structure, Function, and Bioinformatics 50 (3), 437-450, 2003 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u-x6o8ySG0sC Cited by: 5520

The anatomy and taxonomy of protein structure JS Richardson Advances in protein chemistry 34, 167-339, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u5HHmVD_uO8C Cited by: 4573

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix D Liebschner, PV Afonine, ML Baker, G Bunkóczi, VB Chen, TI Croll, … Acta Crystallographica Section D: Structural Biology 75 (10), 861-877, 2019 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:HGTzPopzzJcC Cited by: 4463

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids IW Davis, A Leaver-Fay, VB Chen, JN Block, GJ Kapral, X Wang, … Nucleic acids research 35 (suppl2), W375-W383, 2007 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:d1gkVwhDpl0C Cited by: 4223

MolProbity: more and better reference data for improved all‐atom structure validation CJ Williams, JJ Headd, NW Moriarty, MG Prisant, LL Videau, LN Deis, … Protein Science 27 (1), 293-315, 2018 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:5icHVeHT4IsC Cited by: 3051

Amino acid preferences for specific locations at the ends of α helices JS Richardson, DC Richardson Science 240 (4859), 1648-1652, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:-nhnvRiOwuoC Cited by: 1743

Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation JM Word, SC Lovell, JS Richardson, DC Richardson Journal of molecular biology 285 (4), 1735-1747, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Tyk-4Ss8FVUC Cited by: 1601

The penultimate rotamer library SC Lovell, JM Word, JS Richardson, DC Richardson Proteins: Structure, Function, and Bioinformatics 40 (3), 389-408, 2000 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:IjCSPb-OGe4C Cited by: 1347

Principles and patterns of protein conformation JS Richardson, DC Richardson Prediction of protein structure and the principles of protein conformation, 1-98, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ipzZ9siozwsC Cited by: 1324

Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, KM Beem, JS Richardson, DC Richardson Journal of molecular biology 160 (2), 181-217, 1982 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:UeHWp8X0CEIC Cited by: 1298

Structure and mechanism of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, JS Richardson, DC Richardson Nature 306 (5940), 284-287, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:zYLM7Y9cAGgC Cited by: 1241

MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes IW Davis, LW Murray, JS Richardson, DC Richardson Nucleic acids research 32 (suppl2), W615-W619, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:YsMSGLbcyi4C Cited by: 1115

Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation JS Richardson, DC Richardson Proceedings of the National Academy of Sciences 99 (5), 2754-2759, 2002 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:W7OEmFMy1HYC Cited by: 934

The Phenix software for automated determination of macromolecular structures PD Adams, PV Afonine, G Bunkóczi, VB Chen, N Echols, JJ Headd, … Methods 55 (1), 94-106, 2011 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:z_wVstp3MssC Cited by: 853

Crystal structure of bovine Cu, Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. J Richardson, KA Thomas, BH Rubin, DC Richardson Proceedings of the National Academy of Sciences 72 (4), 1349-1353, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:WF5omc3nYNoC Cited by: 704

Electrostatic recognition between superoxide and copper, zinc superoxide dismutase ED Getzoff, JA Tainer, PK Weiner, PA Kollman, JS Richardson, … Nature 306 (5940), 287-290, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ufrVoPGSRksC Cited by: 701

β-Sheet topology and the relatedness of proteins JS Richardson Nature 268 (5620), 495-500, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:eQOLeE2rZwMC Cited by: 689

Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms JM Word, SC Lovell, TH LaBean, HC Taylor, ME Zalis, BK Presley, … Journal of molecular biology 285 (4), 1711-1733, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:LkGwnXOMwfcC Cited by: 649

Co-authors

David C. Richardson 7P3t1woAAAAJ

Paul D. Adams K08_cxoAAAAJ

Randy J Read BbKCf7UAAAAJ

Jeff Headd UrL7Cv4AAAAJ

Pavel Afonine 5OkzCh8AAAAJ

Ian W. Davis gDtFWBIAAAAJ

Gary Kapral 1f-v9G4AAAAJ

Dr Airlie J. McCoy vdDwlucAAAAJ

Daniel A. Keedy TVaqcVwAAAAJ

Peter Zwart 2yUvzdEAAAAJ

Li-Wei Hung ThQIKZMAAAAJ

Simon Lovell fRg9XLwAAAAJ

Bradley Hintze rcrjTTcAAAAJ

Tristan Croll 3oJcpU8AAAAJ

Jack Snoeyink fIoDWp8AAAAJ

Swati Jain HE6wL6sAAAAJ

Billy K. Poon p-a9soAAAAAJ

Dorothee Liebschner SfjtO7wAAAAJ

John Tainer UWfKH0MAAAAJ

Paul I W de Bakker DTco-eAAAAAJ

Google Scholar

Jane S. Richardson Professor of Biochemistry, Duke University http://kinemage.biochem.duke.edu/ PHENIX: a comprehensive Python-based system for macromolecular structure solution PD Adams, PV Afonine, G Bunkóczi, VB Chen, IW Davis, N Echols, … Acta Crystallographica Section D: Biological Crystallography 66 (2), 213-221, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:qjMakFHDy7sC Cited by: 23685

MolProbity: all-atom structure validation for macromolecular crystallography VB Chen, WB Arendall, JJ Headd, DA Keedy, RM Immormino, GJ Kapral, … Acta Crystallographica Section D: Biological Crystallography 66 (1), 12-21, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Y0pCki6q_DkC Cited by: 14195

Structure validation by Cα geometry: ϕ, ψ and Cβ deviation SC Lovell, IW Davis, WB Arendall III, PIW De Bakker, JM Word, … Proteins: Structure, Function, and Bioinformatics 50 (3), 437-450, 2003 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u-x6o8ySG0sC Cited by: 5520

The anatomy and taxonomy of protein structure JS Richardson Advances in protein chemistry 34, 167-339, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u5HHmVD_uO8C Cited by: 4573

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix D Liebschner, PV Afonine, ML Baker, G Bunkóczi, VB Chen, TI Croll, … Acta Crystallographica Section D: Structural Biology 75 (10), 861-877, 2019 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:HGTzPopzzJcC Cited by: 4463

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids IW Davis, A Leaver-Fay, VB Chen, JN Block, GJ Kapral, X Wang, … Nucleic acids research 35 (suppl2), W375-W383, 2007 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:d1gkVwhDpl0C Cited by: 4223

MolProbity: more and better reference data for improved all‐atom structure validation CJ Williams, JJ Headd, NW Moriarty, MG Prisant, LL Videau, LN Deis, … Protein Science 27 (1), 293-315, 2018 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:5icHVeHT4IsC Cited by: 3051

Amino acid preferences for specific locations at the ends of α helices JS Richardson, DC Richardson Science 240 (4859), 1648-1652, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:-nhnvRiOwuoC Cited by: 1743

Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation JM Word, SC Lovell, JS Richardson, DC Richardson Journal of molecular biology 285 (4), 1735-1747, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Tyk-4Ss8FVUC Cited by: 1601

The penultimate rotamer library SC Lovell, JM Word, JS Richardson, DC Richardson Proteins: Structure, Function, and Bioinformatics 40 (3), 389-408, 2000 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:IjCSPb-OGe4C Cited by: 1347

Principles and patterns of protein conformation JS Richardson, DC Richardson Prediction of protein structure and the principles of protein conformation, 1-98, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ipzZ9siozwsC Cited by: 1324

Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, KM Beem, JS Richardson, DC Richardson Journal of molecular biology 160 (2), 181-217, 1982 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:UeHWp8X0CEIC Cited by: 1298

Structure and mechanism of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, JS Richardson, DC Richardson Nature 306 (5940), 284-287, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:zYLM7Y9cAGgC Cited by: 1241

MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes IW Davis, LW Murray, JS Richardson, DC Richardson Nucleic acids research 32 (suppl2), W615-W619, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:YsMSGLbcyi4C Cited by: 1115

Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation JS Richardson, DC Richardson Proceedings of the National Academy of Sciences 99 (5), 2754-2759, 2002 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:W7OEmFMy1HYC Cited by: 934

The Phenix software for automated determination of macromolecular structures PD Adams, PV Afonine, G Bunkóczi, VB Chen, N Echols, JJ Headd, … Methods 55 (1), 94-106, 2011 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:z_wVstp3MssC Cited by: 853

Crystal structure of bovine Cu, Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. J Richardson, KA Thomas, BH Rubin, DC Richardson Proceedings of the National Academy of Sciences 72 (4), 1349-1353, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:WF5omc3nYNoC Cited by: 704

Electrostatic recognition between superoxide and copper, zinc superoxide dismutase ED Getzoff, JA Tainer, PK Weiner, PA Kollman, JS Richardson, … Nature 306 (5940), 287-290, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ufrVoPGSRksC Cited by: 701

β-Sheet topology and the relatedness of proteins JS Richardson Nature 268 (5620), 495-500, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:eQOLeE2rZwMC Cited by: 689

Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms JM Word, SC Lovell, TH LaBean, HC Taylor, ME Zalis, BK Presley, … Journal of molecular biology 285 (4), 1711-1733, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:LkGwnXOMwfcC Cited by: 649

Co-authors

David C. Richardson googlescholarauthor_id:7P3t1woAAAAJ

Paul D. Adams googlescholarauthorid:K08cxoAAAAJ

Randy J Read googlescholarauthor_id:BbKCf7UAAAAJ

Jeff Headd googlescholarauthor_id:UrL7Cv4AAAAJ

Pavel Afonine googlescholarauthor_id:5OkzCh8AAAAJ

Ian W. Davis googlescholarauthor_id:gDtFWBIAAAAJ

Gary Kapral googlescholarauthor_id:1f-v9G4AAAAJ

Dr Airlie J. McCoy googlescholarauthor_id:vdDwlucAAAAJ

Daniel A. Keedy googlescholarauthor_id:TVaqcVwAAAAJ

Peter Zwart googlescholarauthor_id:2yUvzdEAAAAJ

Li-Wei Hung googlescholarauthor_id:ThQIKZMAAAAJ

Simon Lovell googlescholarauthor_id:fRg9XLwAAAAJ

Bradley Hintze googlescholarauthor_id:rcrjTTcAAAAJ

Tristan Croll googlescholarauthor_id:3oJcpU8AAAAJ

Jack Snoeyink googlescholarauthor_id:fIoDWp8AAAAJ

Swati Jain googlescholarauthor_id:HE6wL6sAAAAJ

Billy K. Poon googlescholarauthor_id:p-a9soAAAAAJ

Dorothee Liebschner googlescholarauthor_id:SfjtO7wAAAAJ

John Tainer googlescholarauthor_id:UWfKH0MAAAAJ

Paul I W de Bakker googlescholarauthor_id:DTco-eAAAAAJ

Google Scholar

Jane S. Richardson Professor of Biochemistry, Duke University http://kinemage.biochem.duke.edu/ PHENIX: a comprehensive Python-based system for macromolecular structure solution PD Adams, PV Afonine, G Bunkóczi, VB Chen, IW Davis, N Echols, … Acta Crystallographica Section D: Biological Crystallography 66 (2), 213-221, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:qjMakFHDy7sC Cited by: 23685

MolProbity: all-atom structure validation for macromolecular crystallography VB Chen, WB Arendall, JJ Headd, DA Keedy, RM Immormino, GJ Kapral, … Acta Crystallographica Section D: Biological Crystallography 66 (1), 12-21, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Y0pCki6q_DkC Cited by: 14195

Structure validation by Cα geometry: ϕ, ψ and Cβ deviation SC Lovell, IW Davis, WB Arendall III, PIW De Bakker, JM Word, … Proteins: Structure, Function, and Bioinformatics 50 (3), 437-450, 2003 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u-x6o8ySG0sC Cited by: 5520

The anatomy and taxonomy of protein structure JS Richardson Advances in protein chemistry 34, 167-339, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u5HHmVD_uO8C Cited by: 4573

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix D Liebschner, PV Afonine, ML Baker, G Bunkóczi, VB Chen, TI Croll, … Acta Crystallographica Section D: Structural Biology 75 (10), 861-877, 2019 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:HGTzPopzzJcC Cited by: 4463

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids IW Davis, A Leaver-Fay, VB Chen, JN Block, GJ Kapral, X Wang, … Nucleic acids research 35 (suppl2), W375-W383, 2007 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:d1gkVwhDpl0C Cited by: 4223

MolProbity: more and better reference data for improved all‐atom structure validation CJ Williams, JJ Headd, NW Moriarty, MG Prisant, LL Videau, LN Deis, … Protein Science 27 (1), 293-315, 2018 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:5icHVeHT4IsC Cited by: 3051

Amino acid preferences for specific locations at the ends of α helices JS Richardson, DC Richardson Science 240 (4859), 1648-1652, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:-nhnvRiOwuoC Cited by: 1743

Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation JM Word, SC Lovell, JS Richardson, DC Richardson Journal of molecular biology 285 (4), 1735-1747, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Tyk-4Ss8FVUC Cited by: 1601

The penultimate rotamer library SC Lovell, JM Word, JS Richardson, DC Richardson Proteins: Structure, Function, and Bioinformatics 40 (3), 389-408, 2000 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:IjCSPb-OGe4C Cited by: 1347

Principles and patterns of protein conformation JS Richardson, DC Richardson Prediction of protein structure and the principles of protein conformation, 1-98, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ipzZ9siozwsC Cited by: 1324

Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, KM Beem, JS Richardson, DC Richardson Journal of molecular biology 160 (2), 181-217, 1982 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:UeHWp8X0CEIC Cited by: 1298

Structure and mechanism of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, JS Richardson, DC Richardson Nature 306 (5940), 284-287, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:zYLM7Y9cAGgC Cited by: 1241

MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes IW Davis, LW Murray, JS Richardson, DC Richardson Nucleic acids research 32 (suppl2), W615-W619, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:YsMSGLbcyi4C Cited by: 1115

Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation JS Richardson, DC Richardson Proceedings of the National Academy of Sciences 99 (5), 2754-2759, 2002 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:W7OEmFMy1HYC Cited by: 934

The Phenix software for automated determination of macromolecular structures PD Adams, PV Afonine, G Bunkóczi, VB Chen, N Echols, JJ Headd, … Methods 55 (1), 94-106, 2011 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:z_wVstp3MssC Cited by: 853

Crystal structure of bovine Cu, Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. J Richardson, KA Thomas, BH Rubin, DC Richardson Proceedings of the National Academy of Sciences 72 (4), 1349-1353, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:WF5omc3nYNoC Cited by: 704

Electrostatic recognition between superoxide and copper, zinc superoxide dismutase ED Getzoff, JA Tainer, PK Weiner, PA Kollman, JS Richardson, … Nature 306 (5940), 287-290, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ufrVoPGSRksC Cited by: 701

β-Sheet topology and the relatedness of proteins JS Richardson Nature 268 (5620), 495-500, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:eQOLeE2rZwMC Cited by: 689

Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms JM Word, SC Lovell, TH LaBean, HC Taylor, ME Zalis, BK Presley, … Journal of molecular biology 285 (4), 1711-1733, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:LkGwnXOMwfcC Cited by: 649

Co-authors

David C. Richardson googlescholarauthorid davidc._richardson.md:7P3t1woAAAAJ

Paul D. Adams googlescholarauthorid pauld.adams.md:K08cxoAAAAJ

Randy J Read googlescholarauthorid randyj_read.md:BbKCf7UAAAAJ

Jeff Headd googlescholarauthorid jeffheadd.md:UrL7Cv4AAAAJ

Pavel Afonine googlescholarauthorid pavelafonine.md:5OkzCh8AAAAJ

Ian W. Davis googlescholarauthorid ianw._davis.md:gDtFWBIAAAAJ

Gary Kapral googlescholarauthorid garykapral.md:1f-v9G4AAAAJ

Dr Airlie J. McCoy googlescholarauthorid drairliej.mccoy.md:vdDwlucAAAAJ

Daniel A. Keedy googlescholarauthorid daniela._keedy.md:TVaqcVwAAAAJ

Peter Zwart googlescholarauthorid peterzwart.md:2yUvzdEAAAAJ

Li-Wei Hung googlescholarauthorid li-weihung.md:ThQIKZMAAAAJ

Simon Lovell googlescholarauthorid simonlovell.md:fRg9XLwAAAAJ

Bradley Hintze googlescholarauthorid bradleyhintze.md:rcrjTTcAAAAJ

Tristan Croll googlescholarauthorid tristancroll.md:3oJcpU8AAAAJ

Jack Snoeyink googlescholarauthorid jacksnoeyink.md:fIoDWp8AAAAJ

Swati Jain googlescholarauthorid swatijain.md:HE6wL6sAAAAJ

Billy K. Poon googlescholarauthorid billyk._poon.md:p-a9soAAAAAJ

Dorothee Liebschner googlescholarauthorid dorotheeliebschner.md:SfjtO7wAAAAJ

John Tainer googlescholarauthorid johntainer.md:UWfKH0MAAAAJ

Paul I W de Bakker googlescholarauthorid pauliwde_bakker.md:DTco-eAAAAAJ

Google Scholar

Jane S. Richardson

Professor of Biochemistry, Duke University

http://kinemage.biochem.duke.edu/

PHENIX: a comprehensive Python-based system for macromolecular structure solution PD Adams, PV Afonine, G Bunkóczi, VB Chen, IW Davis, N Echols, … Acta Crystallographica Section D: Biological Crystallography 66 (2), 213-221, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:qjMakFHDy7sC

MolProbity: all-atom structure validation for macromolecular crystallography VB Chen, WB Arendall, JJ Headd, DA Keedy, RM Immormino, GJ Kapral, … Acta Crystallographica Section D: Biological Crystallography 66 (1), 12-21, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Y0pCki6q_DkC

Structure validation by Cα geometry: ϕ, ψ and Cβ deviation SC Lovell, IW Davis, WB Arendall III, PIW De Bakker, JM Word, … Proteins: Structure, Function, and Bioinformatics 50 (3), 437-450, 2003 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u-x6o8ySG0sC

The anatomy and taxonomy of protein structure JS Richardson Advances in protein chemistry 34, 167-339, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u5HHmVD_uO8C

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix D Liebschner, PV Afonine, ML Baker, G Bunkóczi, VB Chen, TI Croll, … Acta Crystallographica Section D: Structural Biology 75 (10), 861-877, 2019 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:HGTzPopzzJcC

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids IW Davis, A Leaver-Fay, VB Chen, JN Block, GJ Kapral, X Wang, … Nucleic acids research 35 (suppl2), W375-W383, 2007 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:d1gkVwhDpl0C

MolProbity: more and better reference data for improved all‐atom structure validation CJ Williams, JJ Headd, NW Moriarty, MG Prisant, LL Videau, LN Deis, … Protein Science 27 (1), 293-315, 2018 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:5icHVeHT4IsC

Amino acid preferences for specific locations at the ends of α helices JS Richardson, DC Richardson Science 240 (4859), 1648-1652, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:-nhnvRiOwuoC

Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation JM Word, SC Lovell, JS Richardson, DC Richardson Journal of molecular biology 285 (4), 1735-1747, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Tyk-4Ss8FVUC

The penultimate rotamer library SC Lovell, JM Word, JS Richardson, DC Richardson Proteins: Structure, Function, and Bioinformatics 40 (3), 389-408, 2000 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:IjCSPb-OGe4C

Principles and patterns of protein conformation JS Richardson, DC Richardson Prediction of protein structure and the principles of protein conformation, 1-98, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ipzZ9siozwsC

Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, KM Beem, JS Richardson, DC Richardson Journal of molecular biology 160 (2), 181-217, 1982 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:UeHWp8X0CEIC

Structure and mechanism of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, JS Richardson, DC Richardson Nature 306 (5940), 284-287, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:zYLM7Y9cAGgC

MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes IW Davis, LW Murray, JS Richardson, DC Richardson Nucleic acids research 32 (suppl2), W615-W619, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:YsMSGLbcyi4C

Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation JS Richardson, DC Richardson Proceedings of the National Academy of Sciences 99 (5), 2754-2759, 2002 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:W7OEmFMy1HYC

The Phenix software for automated determination of macromolecular structures PD Adams, PV Afonine, G Bunkóczi, VB Chen, N Echols, JJ Headd, … Methods 55 (1), 94-106, 2011 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:z_wVstp3MssC

Crystal structure of bovine Cu, Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. J Richardson, KA Thomas, BH Rubin, DC Richardson Proceedings of the National Academy of Sciences 72 (4), 1349-1353, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:WF5omc3nYNoC

Electrostatic recognition between superoxide and copper, zinc superoxide dismutase ED Getzoff, JA Tainer, PK Weiner, PA Kollman, JS Richardson, … Nature 306 (5940), 287-290, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ufrVoPGSRksC

β-Sheet topology and the relatedness of proteins JS Richardson Nature 268 (5620), 495-500, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:eQOLeE2rZwMC

Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms JM Word, SC Lovell, TH LaBean, HC Taylor, ME Zalis, BK Presley, … Journal of molecular biology 285 (4), 1711-1733, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:LkGwnXOMwfcC

Co-authors

David C. Richardson googlescholarauthorid davidc._richardson.md:7P3t1woAAAAJ

Paul D. Adams googlescholarauthorid pauld.adams.md:K08cxoAAAAJ

Randy J Read googlescholarauthorid randyj_read.md:BbKCf7UAAAAJ

Jeff Headd googlescholarauthorid jeffheadd.md:UrL7Cv4AAAAJ

Pavel Afonine googlescholarauthorid pavelafonine.md:5OkzCh8AAAAJ

Ian W. Davis googlescholarauthorid ianw._davis.md:gDtFWBIAAAAJ

Gary Kapral googlescholarauthorid garykapral.md:1f-v9G4AAAAJ

Dr Airlie J. McCoy googlescholarauthorid drairliej.mccoy.md:vdDwlucAAAAJ

Daniel A. Keedy googlescholarauthorid daniela._keedy.md:TVaqcVwAAAAJ

Peter Zwart googlescholarauthorid peterzwart.md:2yUvzdEAAAAJ

Li-Wei Hung googlescholarauthorid li-weihung.md:ThQIKZMAAAAJ

Simon Lovell googlescholarauthorid simonlovell.md:fRg9XLwAAAAJ

Bradley Hintze googlescholarauthorid bradleyhintze.md:rcrjTTcAAAAJ

Tristan Croll googlescholarauthorid tristancroll.md:3oJcpU8AAAAJ

Jack Snoeyink googlescholarauthorid jacksnoeyink.md:fIoDWp8AAAAJ

Swati Jain googlescholarauthorid swatijain.md:HE6wL6sAAAAJ

Billy K. Poon googlescholarauthorid billyk._poon.md:p-a9soAAAAAJ

Dorothee Liebschner googlescholarauthorid dorotheeliebschner.md:SfjtO7wAAAAJ

John Tainer googlescholarauthorid johntainer.md:UWfKH0MAAAAJ

Paul I W de Bakker googlescholarauthorid pauliwde_bakker.md:DTco-eAAAAAJ

Google Scholar

Jane S. Richardson

Professor of Biochemistry, Duke University

http://kinemage.biochem.duke.edu/

PHENIX: a comprehensive Python-based system for macromolecular structure solution PD Adams, PV Afonine, G Bunkóczi, VB Chen, IW Davis, N Echols, … Acta Crystallographica Section D: Biological Crystallography 66 (2), 213-221, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:qjMakFHDy7sC

MolProbity: all-atom structure validation for macromolecular crystallography VB Chen, WB Arendall, JJ Headd, DA Keedy, RM Immormino, GJ Kapral, … Acta Crystallographica Section D: Biological Crystallography 66 (1), 12-21, 2010 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Y0pCki6q_DkC

Structure validation by Cα geometry: ϕ, ψ and Cβ deviation SC Lovell, IW Davis, WB Arendall III, PIW De Bakker, JM Word, … Proteins: Structure, Function, and Bioinformatics 50 (3), 437-450, 2003 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u-x6o8ySG0sC

The anatomy and taxonomy of protein structure JS Richardson Advances in protein chemistry 34, 167-339, 1981 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:u5HHmVD_uO8C

Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix D Liebschner, PV Afonine, ML Baker, G Bunkóczi, VB Chen, TI Croll, … Acta Crystallographica Section D: Structural Biology 75 (10), 861-877, 2019 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:HGTzPopzzJcC

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids IW Davis, A Leaver-Fay, VB Chen, JN Block, GJ Kapral, X Wang, … Nucleic acids research 35 (suppl2), W375-W383, 2007 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:d1gkVwhDpl0C

MolProbity: more and better reference data for improved all‐atom structure validation CJ Williams, JJ Headd, NW Moriarty, MG Prisant, LL Videau, LN Deis, … Protein Science 27 (1), 293-315, 2018 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:5icHVeHT4IsC

Amino acid preferences for specific locations at the ends of α helices JS Richardson, DC Richardson Science 240 (4859), 1648-1652, 1988 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:-nhnvRiOwuoC

Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation JM Word, SC Lovell, JS Richardson, DC Richardson Journal of molecular biology 285 (4), 1735-1747, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:Tyk-4Ss8FVUC

The penultimate rotamer library SC Lovell, JM Word, JS Richardson, DC Richardson Proteins: Structure, Function, and Bioinformatics 40 (3), 389-408, 2000 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:IjCSPb-OGe4C

Principles and patterns of protein conformation JS Richardson, DC Richardson Prediction of protein structure and the principles of protein conformation, 1-98, 1989 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ipzZ9siozwsC

Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, KM Beem, JS Richardson, DC Richardson Journal of molecular biology 160 (2), 181-217, 1982 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:UeHWp8X0CEIC

Structure and mechanism of copper, zinc superoxide dismutase JA Tainer, ED Getzoff, JS Richardson, DC Richardson Nature 306 (5940), 284-287, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:zYLM7Y9cAGgC

MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes IW Davis, LW Murray, JS Richardson, DC Richardson Nucleic acids research 32 (suppl2), W615-W619, 2004 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1_VRcAAAAJ:YsMSGLbcyi4C

Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation JS Richardson, DC Richardson Proceedings of the National Academy of Sciences 99 (5), 2754-2759, 2002 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:W7OEmFMy1HYC

The Phenix software for automated determination of macromolecular structures PD Adams, PV Afonine, G Bunkóczi, VB Chen, N Echols, JJ Headd, … Methods 55 (1), 94-106, 2011 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:z_wVstp3MssC

Crystal structure of bovine Cu, Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands. J Richardson, KA Thomas, BH Rubin, DC Richardson Proceedings of the National Academy of Sciences 72 (4), 1349-1353, 1975 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:WF5omc3nYNoC

Electrostatic recognition between superoxide and copper, zinc superoxide dismutase ED Getzoff, JA Tainer, PK Weiner, PA Kollman, JS Richardson, … Nature 306 (5940), 287-290, 1983 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:ufrVoPGSRksC

β-Sheet topology and the relatedness of proteins JS Richardson Nature 268 (5620), 495-500, 1977 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:eQOLeE2rZwMC

Visualizing and quantifying molecular goodness-of-fit: small-probe contact dots with explicit hydrogen atoms JM Word, SC Lovell, TH LaBean, HC Taylor, ME Zalis, BK Presley, … Journal of molecular biology 285 (4), 1711-1733, 1999 Link: https://scholar.google.com/citations?viewop=viewcitation&hl=en&user=UF1VRcAAAAJ&citationforview=UF1VRcAAAAJ:LkGwnXOMwfcC

Co-authors

David C. Richardson googlescholarauthorid davidc._richardson.md:7P3t1woAAAAJ

Paul D. Adams googlescholarauthorid pauld.adams.md:K08cxoAAAAJ

Randy J Read googlescholarauthorid randyj_read.md:BbKCf7UAAAAJ

Jeff Headd googlescholarauthorid jeffheadd.md:UrL7Cv4AAAAJ

Pavel Afonine googlescholarauthorid pavelafonine.md:5OkzCh8AAAAJ

Ian W. Davis googlescholarauthorid ianw._davis.md:gDtFWBIAAAAJ

Gary Kapral googlescholarauthorid garykapral.md:1f-v9G4AAAAJ

Dr Airlie J. McCoy googlescholarauthorid drairliej.mccoy.md:vdDwlucAAAAJ

Daniel A. Keedy googlescholarauthorid daniela._keedy.md:TVaqcVwAAAAJ

Peter Zwart googlescholarauthorid peterzwart.md:2yUvzdEAAAAJ

Li-Wei Hung googlescholarauthorid li-weihung.md:ThQIKZMAAAAJ

Simon Lovell googlescholarauthorid simonlovell.md:fRg9XLwAAAAJ

Bradley Hintze googlescholarauthorid bradleyhintze.md:rcrjTTcAAAAJ

Tristan Croll googlescholarauthorid tristancroll.md:3oJcpU8AAAAJ

Jack Snoeyink googlescholarauthorid jacksnoeyink.md:fIoDWp8AAAAJ

Swati Jain googlescholarauthorid swatijain.md:HE6wL6sAAAAJ

Billy K. Poon googlescholarauthorid billyk._poon.md:p-a9soAAAAAJ

Dorothee Liebschner googlescholarauthorid dorotheeliebschner.md:SfjtO7wAAAAJ

John Tainer googlescholarauthorid johntainer.md:UWfKH0MAAAAJ

Paul I W de Bakker googlescholarauthorid pauliwde_bakker.md:DTco-eAAAAAJ










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