Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 4
pubmed:dateCreated
2004-3-24
pubmed:abstractText
Human Rap1GAP, the GTPase-activating protein (GAP) for the small GTPase Rap1, was recombinantly expressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. Crystals were obtained using PEG 3350 as a precipitating agent and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 170.7, b = 224.5, c = 48.7 A. A complete data set was collected to 2.9 A resolution at 100 K using synchrotron radiation. The structure may reveal features of the unique reaction mechanism of Rap1GAP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
752-4
pubmed:dateRevised
2008-5-14
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Purification, crystallization and preliminary structural characterization of human Rap1GAP.
pubmed:affiliation
Max-Planck-Institute für Molekulare Physiologie, Abteilung Strukturbiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't