Purification, crystallization and preliminary structural characterization of human Rap1GAP

Item Type:	Article
Title:	Purification, crystallization and preliminary structural characterization of human Rap1GAP
Creators Name:	Daumke, O. and Wittinghofer, A. and Weyand, M.
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.
Keywords:	Rap1, GTPases, GTPase-activating proteins (GAPs), GTP/GDP-binding proteins
Source:	Acta Crystallographica Section D : Structural Biology
ISSN:	2059-7983
Publisher:	International Union of Crystallography
Volume:	60
Number:	Pt 4
Page Range:	752-4
Date:	April 2004
Official Publication:	https://doi.org/10.1107/s0907444904002392
PubMed:	View item in PubMed

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