Nanoscale mosaicity revealed in peptide microcrystals by scanning electron nanodiffraction.

ABSTRACT: Changes in lattice structure across sub-regions of protein crystals are challenging to assess when relying on whole crystal measurements. Because of this difficulty, macromolecular structure determination from protein micro and nanocrystals requires assumptions of bulk crystallinity and domain block substructure. Here we map lattice structure across micron size areas of cryogenically preserved three-dimensional peptide crystals using a nano-focused electron beam. This approach produces diffraction from as few as 1500 molecules in a crystal, is sensitive to crystal thickness and three-dimensional lattice orientation. Real-space maps reconstructed from unsupervised classification of diffraction patterns across a crystal reveal regions of crystal order/disorder and three-dimensional lattice t

SUBMITTER: Gallagher-Jones M 

PROVIDER: S-EPMC6338664 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature