2O31
Crystal structure of the second SH3 domain from ponsin
Summary for 2O31
| Entry DOI | 10.2210/pdb2o31/pdb |
| Related | 2O2W |
| Descriptor | Ponsin, FORMIC ACID (3 entities in total) |
| Functional Keywords | sh3, ponsin, src homology 3, signaling protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 7790.76 |
| Authors | Pinotsis, N.,Wilmanns, M.,Margiolaki, I. (deposition date: 2006-11-30, release date: 2007-10-23, Last modification date: 2023-10-25) |
| Primary citation | Margiolaki, I.,Wright, J.P.,Wilmanns, M.,Fitch, A.N.,Pinotsis, N. Second SH3 domain of ponsin solved from powder diffraction J.Am.Chem.Soc., 129:11865-11871, 2007 Cited by PubMed Abstract: 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. PubMed: 17784760DOI: 10.1021/ja073846c PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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