Obtaining anomalous and ensemble information from protein crystals from 220 K up to physiological temperatures.

ABSTRACT: X-ray crystallography has been invaluable in delivering structural information about proteins. Previously, an approach has been developed that allows high-quality X-ray diffraction data to be obtained from protein crystals at and above room temperature. Here, this previous work is built on and extended by showing that high-quality anomalous signal can be obtained from single protein crystals using diffraction data collected at 220 K up to physiological temperatures. The anomalous signal can be used to directly determine the structure of a protein, i.e. to phase the data, as is routinely performed under cryoconditions. This ability is demonstrated by obtaining diffraction data from model lysozyme, thaumatin and proteinase K crystals, the anomalous signal from which allowed their structures

SUBMITTER: Doukov T 

PROVIDER: S-EPMC9986799 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature