Protein structure determination by electron diffraction using a single three-dimensional nanocrystal.

ABSTRACT: Three-dimensional nanometre-sized crystals of macromolecules currently resist structure elucidation by single-crystal X-ray crystallography. Here, a single nanocrystal with a diffracting volume of only 0.14 µm³, i.e. no more than 6 × 10⁵ unit cells, provided sufficient information to determine the structure of a rare dimeric polymorph of hen egg-white lysozyme by electron crystallography. This is at least an order of magnitude smaller than was previously possible. The molecular-replacement solution, based on a monomeric polyalanine model, provided sufficient phasing power to show side-chain density, and automated model building was used to reconstruct the side chains. Diffraction data were acquired using the rotation method with parallel beam diffraction on a Titan Kr

SUBMITTER: Clabbers MTB 

PROVIDER: S-EPMC5586247 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature