Crystallization and preliminary X-ray diffraction analysis of the Saccharomyces cerevisiae ran-binding protein Mog1p.
Mog1p binds the Ras-family GTPase Ran/Gsp1p, which has a central role in nucleocytoplasmic transport and cell-cycle progression. Overexpression of MOG1 is able to suppress temperature-sensitive gsp1 mutants in yeast; Deltamog1 null mutants display temperature-sensitive defects in nuclear trafficking. Orthorhombic crystals of bacterially expressed Mog1p that diffract to beyond 2 A resolution using synchrotron radiation have been obtained. The crystals have P2(1)2(1)2(1) symmetry, with unit-cell parameters a = 39.67, b = 51.96, c = 112.23 A, a Matthews coefficient of 2.44 A(3) Da(-1), an estimated solvent content of 49.5% and one chain in the asymmetric unit.
Baker
R P
RP
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, England.
Stewart
M
M
D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014961:X-Ray Diffraction; D020931:ran GTP-Binding Protein / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics
D005656:Fungal Proteins; D020931:ran GTP-Binding Protein