Diffuse X-ray scattering from correlated motions in a protein crystal.

ABSTRACT: Protein dynamics are integral to biological function, yet few techniques are sensitive to collective atomic motions. A long-standing goal of X-ray crystallography has been to combine structural information from Bragg diffraction with dynamic information contained in the diffuse scattering background. However, the origin of macromolecular diffuse scattering has been poorly understood, limiting its applicability. We present a finely sampled diffuse scattering map from triclinic lysozyme with unprecedented accuracy and detail, clearly resolving both the inter- and intramolecular correlations. These correlations are studied theoretically using both all-atom molecular dynamics and simple vibrational models. Although lattice dynamics reproduce most of the diffuse pattern, protein internal dynami

SUBMITTER: Meisburger SP 

PROVIDER: S-EPMC7062842 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature