Ontology highlight
ABSTRACT:
SUBMITTER: Fischer M
PROVIDER: S-EPMC4539595 | biostudies-literature | 2015 Jul
REPOSITORIES: biostudies-literature
Fischer Marcus M Shoichet Brian K BK Fraser James S JS
Chembiochem : a European journal of chemical biology 20150615 11
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 ...[more]