Linked Life Data

15502314

Source:http://linkedlifedata.com/resource/pubmed/id/15502314

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 11
pubmed:dateCreated
2004-10-25
pubmed:abstractText
Regucalcin is a novel calcium ion (Ca(2+)) binding protein that does not contain an EF-hand motif as a Ca(2+)-binding domain and has been demonstrated to play a multi-functional role in many cell types. Human liver regucalcin, consisting of 299 amino-acid residues, was overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method in the presence of polyethylene glycol 4000 as a precipitant. A native crystal diffracted to 2.8 A with synchrotron radiation and belongs to space group P2(1), with unit-cell parameters a = 64.87, b = 52.52, c = 86.38 A, beta = 99.86 degrees . Two molecules most probably exist in the asymmetric unit, corresponding to V(M) = 2.2 A(3) Da(-1). Heavy-atom derivative data were collected and the Pb derivative showed one high-occupancy site per molecule.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2019-21
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Expression, purification, crystallization and preliminary X-ray diffraction studies of human liver regucalcin.
pubmed:affiliation
Exploratory Research Laboratory, Fujisawa Pharmaceutical Co. Ltd, 5-2-3 Tokodai, Tsukuba, Ibaraki 300-2698, Japan. masaichi_warizaya@po.fujisawa.co.jp
pubmed:publicationType
Journal Article