Molecular replacement for small-molecule crystal structure determination from X-ray and electron diffraction data with reduced resolution.

ABSTRACT: The resolution of 3D electron diffraction (ED) data of small-molecule crystals is often relatively poor, due to either electron-beam radiation damage during data collection or poor crystallinity of the material. Direct methods, used as standard for crystal structure determination, are not applicable when the data resolution falls below the commonly accepted limit of 1.2 Å. Therefore an evaluation was carried out of the performance of molecular replacement (MR) procedures, regularly used for protein structure determination, for structure analysis of small-molecule crystal structures from 3D ED data. In the course of this study, two crystal structures of Bi-3812, a highly potent inhibitor of the oncogenic transcription factor BCL6, were determined: the structure of α-Bi-3812 was determined f

SUBMITTER: Gorelik TE 

PROVIDER: S-EPMC10626656 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature