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Three-dimensional diffuse x-ray scattering from crystals of Staphylococcal nuclease.

ABSTRACT: We have developed methods for obtaining and characterizing three-dimensional maps of the reciprocal-space distribution of diffuse x-ray scattering from protein crystals, and have used the methods to study the nature of disorder in crystals of Staphylococcal nuclease. Experimentally obtained maps are 99.5% complete in the reciprocal-space resolution range of 10 A-2.5 A, show symmetry consistent with the P41 space group of the unit cell, and are highly reproducible. Quantitative comparisons of the data with three-dimensional simulations imply liquid-like motions of the protein [Caspar, D. L. D., Clarage, J., Salunke, D. M. & Clarage, M. (1988) Nature (London) 332, 659-662], with a correlation length of 10 A and a root-mean-square displacement of 0.36 A.

SUBMITTER: Wall ME

PROVIDER: S-EPMC21023 | biostudies-literature | 1997 Jun

REPOSITORIES: biostudies-literature

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Three-dimensional diffuse x-ray scattering from crystals of Staphylococcal nuclease.

Wall M E ME Ealick S E SE Gruner S M SM

Proceedings of the National Academy of Sciences of the United States of America 19970601 12

We have developed methods for obtaining and characterizing three-dimensional maps of the reciprocal-space distribution of diffuse x-ray scattering from protein crystals, and have used the methods to study the nature of disorder in crystals of Staphylococcal nuclease. Experimentally obtained maps are 99.5% complete in the reciprocal-space resolution range of 10 A-2.5 A, show symmetry consistent with the P41 space group of the unit cell, and are highly reproducible. Quantitative comparisons of the ...[more]

PMID: 9177191

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