Linked Life Data

9761831

Source:http://linkedlifedata.com/resource/pubmed/id/9761831

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 1
pubmed:dateCreated
1998-11-30
pubmed:abstractText
The NS3 protein of hepatitis C virus (HCV) is thought to be essential for viral replication. The N-terminal domain of the protein contains protease activity and the C-terminal domain contains nucleotide triphosphatase and RNA helicase activity. The RNA helicase domain of HCV NS3 protein was purified by using affinity-column chromatographic methods, and crystallized by using the microbatch crystallization method under oil at 277 K. The crystals belong to primitive trigonal space group P3121 or P3221 with cell dimensions of a = b = 93.3, c = 104.6 A. The asymmetric unit contains one molecule of the helicase domain, with the crystal volume per protein mass (Vm) of 2.50 A3 Da-1 and solvent content of about 50.8% by volume. A native data set to 2.3 A resolution was obtained from a frozen crystal indicating that the crystals are quite suitable for structure determination by multiple isomorphous replacement.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
121-3
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Crystallization and preliminary X-ray crystallographic analysis of the helicase domain of hepatitis C virus NS3 protein.
pubmed:affiliation
Department of Life Sciences, Pohang University of Science of Technology, Pohang, Kyungbuk, 790-784, S. Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't