2o2w
From Proteopedia
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Extending powder diffraction to proteins: structure solution of the second SH3 domain from ponsin
Overview
Determination of protein crystal structures is dependent on the growth of, high-quality single crystals, a process that is not always successful., Optimum crystallization conditions must be systematically sought for, and, microcrystalline powders are frequently obtained in failed attempts to, grow the desired crystal. In materials science, structures of samples, ranging from ceramics, pharmaceuticals, zeolites, etc., can nowadays be, solved, almost routinely, from powdered samples, and there seems to be no, fundamental reason, except the sheer size and complexity of the structures, involved, why powder diffraction should not be employed to solve, structures of small proteins. Indeed, recent work has shown that the, high-quality powder diffraction data can be used in the study of protein, crystal structures. We report the solution, model building, and refinement, of a 67-residue protein domain crystal structure, with a cell volume of 64, 879 A3, from powder diffraction. The second SH3 domain of ponsin, a, protein of high biological significance due to its role in cellular, processes, is determined and refined to resolution limits comparable to, single-crystal techniques. Our results demonstrate the power and future, applicability of the powder technique in structural biology.
About this Structure
2O2W is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Second SH3 domain of ponsin solved from powder diffraction., Margiolaki I, Wright JP, Wilmanns M, Fitch AN, Pinotsis N, J Am Chem Soc. 2007 Sep 26;129(38):11865-71. Epub 2007 Sep 5. PMID:17784760
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