Quantum refinement with multiple conformations: application to the P-cluster in nitrogenase.

ABSTRACT: X-ray crystallography is the main source of atomistic information on the structure of proteins. Normal crystal structures are obtained as a compromise between the X-ray scattering data and a set of empirical restraints that ensure chemically reasonable bond lengths and angles. However, such restraints are not always available or accurate for nonstandard parts of the structure, for example substrates, inhibitors and metal sites. The method of quantum refinement, in which these empirical restraints are replaced by quantum-mechanical (QM) calculations, has previously been suggested for small but interesting parts of the protein. Here, this approach is extended to allow for multiple conformations in the QM region by performing separate QM calculations for each conformation. This approach is sh

SUBMITTER: Cao L 

PROVIDER: S-EPMC7604908 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature