Source:http://linkedlifedata.com/resource/pubmed/id/10089467
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 3
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pubmed:dateCreated |
1999-4-19
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pubmed:abstractText |
Nucleotide-diphospho-sugar transferases represent, in terms of quantity, one of the most important groups of enzymes on Earth, yet little is known about their structure and mechanism. Such a transferase, the spsA gene product involved in the synthesis of the bacterial spore coat in Bacillus subtilis, has been cloned and over-expressed in an Escherichia coli expression system. Crystals have been grown, using PEG 8000 as a precipitant, in a form suitable for high-resolution X-ray analysis. They belong to space group C2221, with unit-cell dimensions a = 42.4, b = 142.0, c = 81.4 A and with one molecule of spsA in the asymmetric unit. The crystals diffract beyond 1.5 A using synchrotron radiation.
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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 |
Mar
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
55
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
677-8
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:10089467-Base Sequence,
pubmed-meshheading:10089467-Cloning, Molecular,
pubmed-meshheading:10089467-Crystallization,
pubmed-meshheading:10089467-Crystallography, X-Ray,
pubmed-meshheading:10089467-DNA Primers,
pubmed-meshheading:10089467-Glycosyltransferases,
pubmed-meshheading:10089467-Recombinant Proteins
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pubmed:year |
1999
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pubmed:articleTitle |
Cloning, crystallization and preliminary X-ray analysis of a nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis.
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pubmed:affiliation |
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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