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• W2070510843 abstract "The structure of carp muscle calcium-binding parvalbumin has been refined to an overall residual, (Σ¦F0 − Fc¦Σ¦F0¦), of 0.25 by a combination of model building and difference Fourier analyses. The atomic positions were allowed to vary up to 0.25 Å from their idealized positions; individual temperature factors ranged from 2 to 150; and 138 solvent peaks were included in this final structure factor calculation. The effects of varying these parameters were analyzed. The treatment of low-order reflections and the influence of solvent have been analyzed in terms of Babinet's principle. These procedures and results are applicable to other protein refinement problems. The errors in co-ordinates are estimated to range from 0.15 Å for the Ca2+ ions to 0.30 Å for internal side chain atoms. A van der Waals' radii study indicates that 42% of the crystal volume is occupied by solvent. There are 16 intermolecular contacts. Of the 108 main chain peptide hydrogen atoms, 15 are neither in contact with solvent nor involved in hydrogen bonds. These “lost” hydrogen bonds are considered to be important to the proposed model of function." @default.
• W2070510843 created "2016-06-24" @default.
• W2070510843 creator A5035694899 @default.
• W2070510843 creator A5079640663 @default.
• W2070510843 date "1975-01-01" @default.
• W2070510843 modified "2023-10-10" @default.
• W2070510843 title "Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference fourier analysis" @default.
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• W2070510843 doi "https://doi.org/10.1016/0022-2836(75)90160-6" @default.
• W2070510843 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1237625" @default.
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