Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition.

ABSTRACT: The Protein Data Bank (PDB) contains a growing number of models that have been determined using neutron diffraction or a hybrid method that combines X-ray and neutron diffraction. The advantage of neutron diffraction experiments is that the positions of all atoms can be determined, including H atoms, which are hardly detectable by X-ray diffraction. This allows the determination of protonation states and the assignment of H atoms to water molecules. Because neutrons are scattered differently by hydrogen and its isotope deuterium, neutron diffraction in combination with H/D exchange can provide information on accessibility, dynamics and chemical lability. In this study, the deposited data, models and model-to-data fit for all PDB entries that used neutron diffraction as the source of experi

SUBMITTER: Liebschner D 

PROVIDER: S-EPMC6079631 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature