Source:http://linkedlifedata.com/resource/pubmed/id/12876358
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 8
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pubmed:dateCreated |
2003-7-23
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pubmed:abstractText |
p47(phox) is a cytosolic component of the phagocyte NADPH oxidase, which is responsible for the production of the superoxide which kills invasive microorgamisms. A recombinant form of a histidine-tagged tandem SH3 domain of the p47(phox)-containing polybasic autoinhibited region was expressed in Escherichia coli and purified and crystallized by the sitting-drop vapour-diffusion method at 293 K using polyethylene glycol 6000 as a precipitant. Diffraction data were collected to 2.15 A resolution at 100 K using synchrotron radiation. The crystal belongs to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 100.02, c = 44.94 A. The presence of one molecule per asymmetric unit gives a crystal volume per protein mass (V(M)) of 2.6 A(3) Da(-1) and a solvent content of 52% by volume.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1479-80
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:12876358-Crystallography, X-Ray,
pubmed-meshheading:12876358-Escherichia coli,
pubmed-meshheading:12876358-Humans,
pubmed-meshheading:12876358-NADPH Oxidase,
pubmed-meshheading:12876358-Phosphoproteins,
pubmed-meshheading:12876358-Protein Structure, Tertiary,
pubmed-meshheading:12876358-Recombinant Proteins,
pubmed-meshheading:12876358-X-Ray Diffraction,
pubmed-meshheading:12876358-src Homology Domains
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pubmed:year |
2003
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pubmed:articleTitle |
Crystallization and preliminary crystallographic analysis of the autoinhibited form of the tandem SH3 domain of p47(phox).
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pubmed:affiliation |
Department of Structural Biology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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