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2Q4P

Ensemble refinement of the crystal structure of protein from Mus musculus Mm.29898

Summary for 2Q4P
Entry DOI10.2210/pdb2q4p/pdb
DescriptorProtein RS21-C6 (2 entities in total)
Functional Keywordsensemble refinement, refinement methodology development, mm.29898, bc004623, 2410015n17rik, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, unknown function
Biological sourceMus musculus (house mouse)
Cellular locationCytoplasm: Q9QY93
Total number of polymer chains2
Total formula weight37821.35
Authors
Levin, E.J.,Kondrashov, D.A.,Wesenberg, G.E.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2007-05-31, release date: 2007-06-19, Last modification date: 2024-10-16)
Primary citationLevin, E.J.,Kondrashov, D.A.,Wesenberg, G.E.,Phillips, G.N.
Ensemble refinement of protein crystal structures: validation and application.
Structure, 15:1040-1052, 2007
Cited by
PubMed Abstract: X-ray crystallography typically uses a single set of coordinates and B factors to describe macromolecular conformations. Refinement of multiple copies of the entire structure has been previously used in specific cases as an alternative means of representing structural flexibility. Here, we systematically validate this method by using simulated diffraction data, and we find that ensemble refinement produces better representations of the distributions of atomic positions in the simulated structures than single-conformer refinements. Comparison of principal components calculated from the refined ensembles and simulations shows that concerted motions are captured locally, but that correlations dissipate over long distances. Ensemble refinement is also used on 50 experimental structures of varying resolution and leads to decreases in R(free) values, implying that improvements in the representation of flexibility observed for the simulated structures may apply to real structures. These gains are essentially independent of resolution or data-to-parameter ratio, suggesting that even structures at moderate resolution can benefit from ensemble refinement.
PubMed: 17850744
DOI: 10.1016/j.str.2007.06.019
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.32 Å)
Structure validation

226707

數據於2024-10-30公開中

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