Highly constrained multiple-copy refinement of protein crystal structures

Autor:	M, Pellegrini, N, Grønbech-Jensen, J A, Kelly, G M, Pfluegl, T O, Yeates
Rok vydání:	1997
Předmět:	Models Molecular Mice Neurotrophin 3 Glutamate-Ammonia Ligase Protein Conformation Normal Distribution Animals Humans Computer Simulation Nerve Growth Factors Crystallography X-Ray
Zdroj:	Proteins. 29(4)
ISSN:	0887-3585
Popis:	In the course of refining atomic protein structures, one often encounters difficulty with molecules that are unusually flexible or otherwise disordered. We approach the problem by combining two relatively recent developments: simultaneous refinement of multiple protein conformations and highly constrained refinement. A constrained Langevin dynamics refinement is tested on two proteins: neurotrophin-3 and glutamine synthetase. The method produces closer agreement between the calculated and observed scattering amplitudes than standard, single-copy, Gaussian atomic displacement parameter refinement. This is accomplished without significantly increasing the number of fitting parameters in the model. These results suggest that loop motion in proteins within a crystal lattice can be extensive and that it is poorly modeled by isotropic Gaussian distributions for each atom.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::dcbf2bae84527673317368a6e8358b28 https://pubmed.ncbi.nlm.nih.gov/9408940 Zobrazit plný text záznamu Plný text