Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 7
pubmed:dateCreated
2011-7-28
pubmed:abstractText
SARS coronavirus (SARS-CoV) is the aetiological agent of the highly infectious severe acute respiratory syndrome (SARS). To gain a better understanding of SARS-CoV replication and transcription proteins, a preliminary X-ray crystallographic study of the C-terminal domain of SARS-CoV nonstructural protein 2 (nsp2) is reported here. The C-terminal domain of SARS-CoV nsp2 was cloned, overexpressed, purified and crystallized using polyethylene glycol 5000 monomethyl ether as the precipitant; the crystals diffracted to 2.5?Å resolution. The crystals belonged to space group P6(5), with unit-cell parameters a=b=112.8, c=91.1?Å, ?=?=90, ?=120°. One molecule is assumed to be present per asymmetric unit, which gives a Matthews coefficient of 2.89?Å3?Da(-1) and a solvent content of 56.2%.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
790-3
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Expression, crystallization and preliminary crystallographic study of the C-terminal half of nsp2 from SARS coronavirus.
pubmed:affiliation
National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't