Conformational variation of proteins at room temperature is not dominated by radiation damage.

ABSTRACT: Protein crystallography data collection at synchrotrons is routinely carried out at cryogenic temperatures to mitigate radiation damage. Although damage still takes place at 100 K and below, the immobilization of free radicals increases the lifetime of the crystals by approximately 100-fold. Recent studies have shown that flash-cooling decreases the heterogeneity of the conformational ensemble and can hide important functional mechanisms from observation. These discoveries have motivated increasing numbers of experiments to be carried out at room temperature. However, the trade-offs between increased risk of radiation damage and increased observation of alternative conformations at room temperature relative to cryogenic temperature have not been examined. A considerable amount of effort ha

SUBMITTER: Russi S 

PROVIDER: S-EPMC5182021 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature