Purification, crystallization and preliminary structural characterization of human Rap1GAP.
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.
Daumke
Oliver
O
Max-Planck-Institute für Molekulare Physiologie, Abteilung Strukturbiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Wittinghofer
Alfred
A
Weyand
Michael
M
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D020690:GTPase-Activating Proteins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D020125:Mutation, Missense
D020690:GTPase-Activating Proteins; C484658:RAP1GAP protein, human