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PDBsum entry 2o31
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Signaling protein
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PDB id
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2o31
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References listed in PDB file
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Key reference
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Title
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Second sh3 domain of ponsin solved from powder diffraction.
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Authors
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I.Margiolaki,
J.P.Wright,
M.Wilmanns,
A.N.Fitch,
N.Pinotsis.
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Ref.
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J Am Chem Soc, 2007,
129,
11865-11871.
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PubMed id
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Abstract
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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.
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