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SSRL Structural Molecular Biology Summer School 2003September 16-19, 2003 |
ParticipantsCourse OrganizersHiro Tsuruta, Ph.D., is a Senior Scientist at SSRL. His research activities mainly focus on structural studies of oligomeric proteins and macromolecular assemblies primarily by non-crystalline x-ray scattering techniques. Serena DeBeer George, Ph.D., is a Beam Line Scientist at the Stanford Synchrotron Radiation Laboratory. Her research focuses on the use of X-ray absorption spectroscopy to elucidate the electronic and geometric structure of bioinorganic and organometallic systems. Ana Gonzalez, Ph.D., is a Staff Scientist
at SSRL. Research interests: Structural studies of proteins and
methods for automation of data collection in macromolecular
crystallography.
Paul Adams, Ph.D., is a Staff Scientist at Lawrence Berkeley
National Laboratory. Research interests: developing new software
for automated crystallographic structure determination and data
collection. Ninian Blackburn, Ph.D., a Professor at the Oregon Graduate Institute. His areas of expertise include structure and function of oxidase and oxygenase metalloenzymes; spectroscopy of metal sites in proteins with emphasis on EPR, EXAFS, absorption edge, and FTIR spectroscopies; coordination chemistry and biochemistry of copper. Biochemistry of metal trafficking in cells. Ashley Deacon Britt Hedman, Ph.D., is a Professor at SSRL. She has ~20
years experience with synchrotron radiation research, in particular
x-ray absorption spectroscopy. Her current research interests
focus on enzyme active site electronic and geometric structure
using ligand and metal XAS. Keith Hodgson, Ph.D., is the Howard H. and Jessie T. Watkins Stanford University Professor of Chemistry and SSRL Director. He is a pioneer in synchrotron-based biological research: performed the world's first SR protein crystal diffraction measurements; explored anomalous dispersion in what later became known as MAD; developed XAS for structural biology; and made early seminal contributions to biological SAXS. John E. Johnson, Ph.D., is Professor, Laboratory of Structural and Molecular Virology at The Scripps Research Institute (TSRI) in La Jolla, California. Using biophysical techniques such as X-ray crystallography and cryoelectron microscopy, Dr. Johnson and his colleagues have gained a better understanding of virus structure and how viruses infect their hosts. This has led to exploration of ways of using molecular biology, mass spectrometry, and biochemical techniques to further understand particle assembly, maturation, and cell entry for insect, plant, and bacteriophage viruses. Irimpan Mathews, Ph.D., is a Staff Scientist at SSRL. Research interests include analysis of structure-function relationships in proteins and structure-based drug discovery. Matthew Newville,
Ph.D., is a Staff Scientist for the University of Chicago at the
Advanced Photon Source. His research interests include fundamental
aspects of x-ray absorption fine-structure spectroscopy and the
application of XAFS to studies of local atomic structures of disordered
systems in material, earth, and environmental sciences.
James Penner-Hahn, Ph.D., is a Professor of Chemistry and
Chair of the Biophysics Research Division at the University of
Michigan. His research focuses on characterization of the active
sites of Zn- and Mn-containing proteins.
Robert Scott, Ph.D., is Distinguished Research Professor
in the Department of Chemistry, University of Georgia. He has
nearly 25 years of experience in the application of x-ray absorption
spectroscopy to biological systems. Recent emphasis is on metal
sensor and DNA-binding proteins involved in transcription and
(metallo) regulation. Dmitri Svergun, Ph.D., is a Team Leader at the European Molecular Biology Laboratory, Hamburg Outstation. Research interests include structure determination of biological macromolecules from synchrotron x-ray and neutron small-angle scattering data.
Les Tari,
Ph.D. Patrice Vachette, Ph.D., is a Staff Scientist at the French synchrotron facility LURE (Orsay near Paris). Interest in the study of conformational changes and assembly mechanisms of biological systems in solution such as proteins, notably allosteric enzymes, and virus particles, both at equilibrium and kinetically, using primarily synchrotron SAXS. Bill Weis, Ph.D., is an Associate Professor of Structural Biology and SSRL, and Director of the Biophysics Program at Stanford University. Research interests include cell membrane recognition, targeting, and adhesion processes studied by crystallographic structure determination and physical biochemistry.
StudentsLuisa Andruzzi, Oregon Health & Science University Rachel Behan, Penn State University Michaeleen Callahan, UC Berkeley Devin Close, University of Utah Jason Davies, Stanford University School of Medicine Frederic Fellouse, Genentech Kelly Gaffney, SSRL Mehmet Karabiyik, The University of Michigan Bonnie Leung, University of Calgary Kari Lunder, Pennsylvania State University Henry Maun, University of Freiburg/Genentech Yvonne Newhouse, Gladstone Institutes David Pettigrew, Oxford University Michael Pushie, University of Calgary Kianoush Sadre-Bazzaz, University of Utah Wen-Jun Shen, Stanford University Jining Wang, Stanford University Matthew Worthington, Indiana University
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