2o2w | pdb_00002o2w

Extending powder diffraction to proteins: structure solution of the second SH3 domain from ponsin

spinqualitylabelsall models 2o2w, resolution 2.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2o2w is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray powder diffraction, Resolution 2.27Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SRBS1_HUMAN Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity).[UniProtKB:Q62417] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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