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• W2795104011 abstract "Protein crystal structures are potentially over-interpreted since they are routinely refined without any restraint on the upper limit of atomic B-factors. Consequently, some of their atoms, undetected in the electron density maps, are allowed to reach extremely large B-factors, even above 100 square Angstroms, and their final positions are purely speculative and not based on any experimental evidence. A strategy to define B-factors upper limits is described here, based on the analysis of protein crystal structures deposited in the Protein Data Bank prior 2008, when the tendency to allow B-factor to arbitrary inflate was limited. This B-factor upper limit (B_max) is determined by extrapolating the relationship between crystal structure average B-factor and percentage of crystal volume occupied by solvent (pcVol) to pcVol =100%, when, ab absurdo, the crystal contains only liquid solvent, the structure of which is, by definition, undetectable in electron density maps. It is thus possible to highlight structures with average B-factors larger than B_max, which should be considered with caution by the users of the information deposited in the Protein Data Bank, in order to avoid scientifically deleterious over-interpretations." @default.
• W2795104011 created "2018-04-06" @default.
• W2795104011 creator A5069990985 @default.
• W2795104011 date "2018-02-23" @default.
• W2795104011 modified "2023-10-15" @default.
• W2795104011 title "How large B-factors can be in protein crystal structures" @default.
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• W2795104011 doi "https://doi.org/10.1186/s12859-018-2083-8" @default.
• W2795104011 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5824579" @default.
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• W2795104011 hasPublicationYear "2018" @default.
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