The purification and crystallization of mDia1 in complex with RhoC.
An N-terminal construct of mouse mDia1 was recombinantly expressed in Escherichia coli, purified and crystallized in complex with truncated human RhoC using the hanging-drop vapour-diffusion method. Crystals were obtained using PEG 2K MME and MgSO4 as a precipitating agent and belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 148.4, b = 85.2, c = 123.2 A. Complete native and SeMet-derivative data sets were collected at 100 K to 3.0 and 3.4 A resolution, respectively, using synchrotron radiation.
Rose
Rolf
R
Department of Structural Biology, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
Wittinghofer
Alfred
A
Weyand
Michael
M
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D000080865:Formins; D006801:Humans; D051379:Mice; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D017384:Sequence Deletion; D017356:Synchrotrons; D018631:ras Proteins; D020741:rho GTP-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D000075024:rhoC GTP-Binding Protein
D002352:Carrier Proteins; C491464:Diap1 protein, mouse; D000080865:Formins; D011994:Recombinant Proteins; C066690:RHOC protein, human; C512911:Rhoc protein, mouse; D018631:ras Proteins; D020741:rho GTP-Binding Proteins; D000075024:rhoC GTP-Binding Protein