Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
1999-4-19
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
677-8
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Cloning, crystallization and preliminary X-ray analysis of a nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis.
pubmed:affiliation
Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5DD, England.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't