Source:http://linkedlifedata.com/resource/pubmed/id/15039575
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 4
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pubmed:dateCreated |
2004-3-24
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0907-4449
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
752-4
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pubmed:dateRevised |
2008-5-14
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pubmed:meshHeading | |
pubmed:year |
2004
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pubmed:articleTitle |
Purification, crystallization and preliminary structural characterization of human Rap1GAP.
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pubmed:affiliation |
Max-Planck-Institute für Molekulare Physiologie, Abteilung Strukturbiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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