Accessing protein conformational ensembles using room-temperature X-ray crystallography
University of California, Berkeley · SLAC National Accelerator Laboratory · +4 more institutions
Abstract
Modern protein crystal structures are based nearly exclusively on X-ray data collected at cryogenic temperatures (generally 100 K). The cooling process is thought to introduce little bias in the functional interpretation of structural results, because cryogenic temperatures minimally perturb the overall protein backbone fold. In contrast, here we show that flash cooling biases previously hidden structural ensembles in protein crystals. By analyzing available data for 30 different proteins using new computational tools for electron-density sampling, model refinement, and molecular packing analysis, we found that crystal cryocooling remodels the conformational distributions of more than 35% of side chains and…
Citation impact
- FWCI
- 12.90
- Percentile
- 100%
- References
- 46
Authors
7- JSJames S. FraserCorresponding
University of California, Berkeley
- HVHenry van den Bedem
SLAC National Accelerator Laboratory, Joint Center for Structural Genomics, Stanford Synchrotron Radiation Lightsource
- AJAvi J. Samelson
University of California, Berkeley
- PTP. Therese Lang
University of California, Berkeley
- JMJames M. Holton
Lawrence Berkeley National Laboratory, University of California, San Francisco
Topics & keywords
- Allosteric regulation
- Crystallography
- Protein crystallization
- Protein structure
- Crystal structure
- Chemistry
- Structural biology
- Protein Data Bank