Source:http://linkedlifedata.com/resource/pubmed/id/11914508
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 4
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pubmed:dateCreated |
2002-3-26
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pubmed:abstractText |
Streptococcal protease precursor, secreted by the human pathogen Streptococcus pyogenes, becomes activated to a cysteine protease. The precursor and the mature enzyme appear to contribute to S. pyogenes virulence. The precursor protein was crystallized in the form of very thin flexible flakes. X-ray diffraction data were collected to 3.15 A resolution at 100 K using synchrotron radiation. The crystals are monoclinic, space group P2(1), with unit-cell parameters a = 41.6, b = 136.0, c = 156.7 A, beta = 95.7 degrees, and contain four copies of the protein in the asymmetric unit.
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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 |
Apr
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
58
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
723-6
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading | |
pubmed:year |
2002
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pubmed:articleTitle |
Crystallization and preliminary crystallographic studies of Streptococcus pyogenes cysteine protease precursor.
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pubmed:affiliation |
Department of Crystallography, Faculty of Chemistry, A. Mickiewicz University, Grunwaldzka 6, 60-780 Poznan, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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