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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2010-3-8
pubmed:abstractText
Streptococcus pneumoniae SP0987, which was identified as a hypothetical protein, has a very low sequence identity to other well characterized lysozyme structures. Since determination of three-dimensional structure is a powerful means of functional characterization, X-ray crystallography has been used to accomplish this task. Here, the expression, purification, crystallization and preliminary crystallographic analysis of SP0987 from Streptococcus pneumoniae TIGR4 are reported. The crystal belonged to space group P2(1)2(1)2(1) (with unit-cell parameters a = 36.46, b = 40.89, c = 147.44 A) and diffracted to a resolution of 1.85 A. The crystals are most likely to contain one molecule in the asymmetric unit, with a V(M) value of 2.02 A(3) Da(-1).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
286-8
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Purification, crystallization and preliminary X-ray studies of the putative lysozyme SP0987 from Streptococcus pneumoniae.
pubmed:affiliation
Key Laboratory of Molecular Biology of Infectious Diseases, Chongqing Medical University, YiXueYuanlu-1, Chongqing 400016, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't