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PubMed · 10425674

Selenium-based MAD phasing: setting the sites on larger structures.

A M Deacon·S E Ealick
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Models, MolecularProtein ConformationSeleniumX-Ray DiffractionJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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A M Deacon, S E Ealick. 1999-07-15. Selenium-based MAD phasing: setting the sites on larger structures.. https://doi.org/10.1016/s0969-2126(99)80096-3

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PubMed2001

Identification of protein oligomerization states by analysis of interface conservation.

The discrimination of true oligomeric protein-protein contacts from nonspecific crystal contacts remains problematic. Criteria that have been used previously base the assignment of oligomeric state on consideration of the area of the interface and/or the results of scoring functions based on statistical potentials. Both techniques have a high success rate but fail in more than 10% of cases. More importantly, the oligomeric states of several proteins are incorrectly assigned by both methods. Here we test the hypothesis that true oligomeric contacts should be identifiable on the basis of an increased degree of conservation of the residues involved in the interface. By quantifying the degree of conservation of the interface and comparing it with that of the remainder of the protein surface, we develop a new criterion that provides a highly effective complement to existing methods.

Models, Molecular↗