Identifying dynamic, partially occupied residues using anomalous scattering.

ABSTRACT: Although often presented as taking single `snapshots' of the conformation of a protein, X-ray crystallography provides an averaged structure over time and space within the crystal. The important but difficult task of characterizing structural ensembles in crystals is typically limited to small conformational changes, such as multiple side-chain conformations. A crystallographic method was recently introduced that utilizes residual electron and anomalous density (READ) to characterize structural ensembles encompassing large-scale structural changes. Key to this method is an ability to accurately measure anomalous signals and distinguish them from noise or other anomalous scatterers. This report presents an optimized data-collection and analysis strategy for partially occupied iodine anomalo

SUBMITTER: Rocchio S 

PROVIDER: S-EPMC6889914 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature