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Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):752-4. Epub 2004 Mar 23.

Purification, crystallization and preliminary structural characterization of human Rap1GAP.

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1
Max-Planck-Institute für Molekulare Physiologie, Abteilung Strukturbiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.

Abstract

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.

PMID:
15039575
DOI:
10.1107/S0907444904002392
[Indexed for MEDLINE]
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