Linked Life Data

9757118

Source:http://linkedlifedata.com/resource/pubmed/id/9757118

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 5
pubmed:dateCreated
1998-12-14
pubmed:abstractText
The trimeric signal-transduction protein GlnK, from Escherichia coli, has been over-expressed, purified to homogeneity and crystallized. The crystals belong to space group P213 with a = 85.53 A and have two subunits in the asymmetric unit. The complex of GlnK with ATP crystallized in space group P63 with a = 57.45 and c = 54.79 A. These crystals have a single subunit in the asymmetric unit. High-quality diffraction data from crystals of GlnK and the GlnK complex have been collected to 2.0 A.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
54
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
996-8
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Crystallization and preliminary X-ray analysis of Escherichia coli GlnK.
pubmed:affiliation
Research School of Chemistry, Australian National University, Canberra ACT 0200, Australia.
pubmed:publicationType
Journal Article