High-Resolution Electron Diffraction of Hydrated Protein Crystals at Room Temperature.

ABSTRACT: Structural characterization is crucial to understanding protein function. Compared with X-ray diffraction methods, electron crystallography can be performed on nanometer-sized crystals and can provide additional information from the resulting Coulomb potential map. Whereas electron crystallography has successfully resolved three-dimensional structures of vitrified protein crystals, its widespread use as a structural biology tool has been limited. One main reason is the fragility of such crystals. Protein crystals can be easily damaged by mechanical stress, change in temperature, or buffer conditions as well as by electron irradiation. This work demonstrates a methodology to preserve these nanocrystals in their natural environment at room temperature for electron diffraction experiments as

SUBMITTER: Plana-Ruiz S 

PROVIDER: S-EPMC10753879 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature