One Crystal, Two Temperatures [electronic resource] : Cryocooling Penalties Alter Ligand Binding to Transient Protein Sites
- Published
- Washington, D.C. : United States. Dept. of Energy. Office of Basic Energy Sciences, 2015.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy - Physical Description
- pages 1,560-1,564 : digital, PDF file
- Additional Creators
- United States. Department of Energy. Office of Basic Energy Sciences, National Institutes of Health (U.S.), and United States. Department of Energy. Office of Scientific and Technical Information
Access Online
- Restrictions on Access
- Free-to-read Unrestricted online access
- Summary
- Interrogating fragment libraries by X-ray crystallography is a powerful strategy for discovering allosteric ligands for protein targets. Cryocooling of crystals should theoretically increase the fraction of occupied binding sites and decrease radiation damage. However, it might also perturb protein conformations that can be accessed at room temperature. Using data from crystals measured consecutively at room temperature and at cryogenic temperature, we found that transient binding sites could be abolished at the cryogenic temperatures employed by standard approaches. Finally, changing the temperature at which the crystallographic data was collected could provide a deliberate perturbation to the equilibrium of protein conformations and help to visualize hidden sites with great potential to allosterically modulate protein function.
- Report Numbers
- E 1.99:1343096
- Subject(s)
- Other Subject(s)
- Note
- Published through SciTech Connect.
05/28/2015.
ChemBioChem: a European journal of chemical biology 16 11 ISSN 1439-4227 AM
Marcus Fischer; Brian K. Shoichet; James S. Fraser.
Univ. of California, San Francisco, CA (United States) - Funding Information
- AC02-05CH11231
GM59957
OD009180
GM110580
STC-1231306
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