Linked Life Data

15299918

Source:http://linkedlifedata.com/resource/pubmed/id/15299918

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 4
pubmed:dateCreated
2004-8-9
pubmed:abstractText
The calcium-binding domain of the small subunit of porcine calpain (domain VI) has been expressed in Escherichia coli, purified, and crystallized in the presence of Ca(2+). Two crystal forms have been obtained by the vapor-diffusion method using PEG 6000 as the precipitant. Crystal form I, belonging to trigonal space group P3(1)21 (or P3(2)21) with cell dimensions a = b = 79.8, c = 57.08 A, alpha = beta = 90.0 and gamma, = 120.0 degrees diffracted to 2.8 A. The second crystal form diffracts to 1.8 A and belongs to monoclinic space group P2(1) with cell dimensions a = 50.1, b = 79.7, c = 57.1 A and beta = 91.2 degrees.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Jul
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
474-6
pubmed:dateRevised
2007-7-24
pubmed:year
1997
pubmed:articleTitle
Purification, crystallization and preliminary X-ray diffraction studies of recombinant calcium-binding domain of the small subunit of porcine calpain.
pubmed:affiliation
Center for Macromolecular Crystallography, University of Alabama at Birmingham, USA.
pubmed:publicationType
Journal Article