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October 7, 2009
2009 Nobel Winner
Was Early User of BioCARS
One of the three winners of the 2009 Nobel Prize in Chemistry, Thomas Steitz, has conducted research at BioCARS. Steitz of Yale University, Ada Yonath of Israel's Weizmann Institute, and Venkatraman Ramakrishnan of Cambridge, England's Medical Research Center shared the award for their study of the structure and function of the ribosome. The following are publications by Steitz based on data taken at BioCARS.
- Kamtekar, Satwik, W. Dexter Kennedy, Jimin Wang, Constantinos Stathopoulos, Dieter Söll, Thomas A. Steitz "The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases", PNAS 100 (4) 1673-1678 (2003).
- Li, Fang, Yong Xiong, Jimin Wang, HyunDae D. Cho, Kozo Tomita, Alan M. Weiner, Thomas A. Steitz "Crystal Structures of the Bacillus stearothermophilus CCA-Adding Enzyme and Its Complexes with ATP or CTP", Cell 111 (6) 815-824 (2002).
- Xiong, Yong, Fang Li, Jimin Wang, Alan M. Weiner, Thomas A. Steitz "Crystal Structures of an Archaeal Class I CCA-Adding Enzyme and Its Nucleotide Complexes", Mol. Cell 12 1165-1172 (2003).
October 6, 2009, Proceedings of the National Academy of Sciences
Natural and recombinant prion structure from X-ray fiber diffraction
A collaboration between scientists at Vanderbilt University and the University of California, San Francisco has led to the first direct information about the molecular structure of prions. Prions are the infectious proteins responsible for human Creutzfeldt-Jakob disease, bovine spongiform encephalopathy, or "mad cow" disease, scrapie in sheep and several other related nervous system disorders in mammals.
In addition, the study has revealed surprisingly large structural differences between natural prions and the closest analogs that scientists have created in the lab. Recombinant prions do not show the same degree of infectious behavior as their natural counterparts. "We expected to find subtle [structural] differences, but we found major differences instead," said Gerald Stubbs, professor of biological sciences at Vanderbilt University. "Although we cannot say for certain that the differences we've seen can explain why natural prions are so infectious, there is a good chance that they are closely related." The work was conducted at BioCARS biosafety level 2 (BSL-2) facilities under an agreement with BioCAT (APS sector 18).
- Full story
- Holger Wille, Wen Bian, Michele McDonald, Amy Kendall, David W. Colby, Lillian Bloch, Julian Ollesch, Alexander L. Borovinskiy, Fred E. Cohen, Stanley B. Prusiner, and Gerald Stubbs
Natural and synthetic prion structure from X-ray fiber diffraction
PNAS, 2009; 106:16990-16995
Facility News
Workshop Participants
December 18, 2008
Workshop on Time-Resolved Crystallography Concludes Successfully
BioCARS hosted a three-day workshop on time-resolved crystallography and Laue diffraction (November 20-22, 2008). Thirty-one participants represented 21 research groups. The international user community was represented by participants from the Czech Republic, Denmark, Canada, and Australia. Many participants left the workshop with plans for designing time-resolved experiments on their own biological systems.