Helmholtz Gemeinschaft

Search
Browse
Statistics
Feeds

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., 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

Repository Staff Only: item control page

Open Access
MDC Library