Validation of electron-microscopy maps using solution small-angle X-ray scattering.

ABSTRACT: The determination of the atomic resolution structure of biomacromolecules is essential for understanding details of their function. Traditionally, such a structure determination has been performed with crystallographic or nuclear resonance methods, but during the last decade, cryogenic transmission electron microscopy (cryo-TEM) has become an equally important tool. As the blotting and flash-freezing of the samples can induce conformational changes, external validation tools are required to ensure that the vitrified samples are representative of the solution. Although many validation tools have already been developed, most of them rely on fully resolved atomic models, which prevents early screening of the cryo-TEM maps. Here, a novel and automated method for performing such a validation ut

SUBMITTER: Lytje K 

PROVIDER: S-EPMC11220840 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature