Structural highlights
Publication Abstract from PubMed
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.
Three-dimensional diffuse x-ray scattering from crystals of Staphylococcal nuclease.,Wall ME, Ealick SE, Gruner SM Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6180-4. PMID:9177191[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wall ME, Ealick SE, Gruner SM. Three-dimensional diffuse x-ray scattering from crystals of Staphylococcal nuclease. Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6180-4. PMID:9177191
