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EC Number
Crystallization
Reference
; dihydroorotate dehydrogenase A, complexed with orotate
; hanging drop vapor diffusion technique, 30% polyethylene glycol, 0.2 M sodium acetate, 0.1 M Tris-HCl, pH 8.5, monoclinic crystals, space group P21
wild-type enzyme and mutants N67A, K213E, P56A, R57A, K136E
in complex with product orotate
by sitting-drop vapor-diffusion technique, to 2.4 A resolution
crystals of the TcDHOD–orotate complex are grown at 4°C by the sitting-drop vapour-diffusion technique using polyethylene glycol 3350 as a precipitant. The crystals diffract to better than 1.8 A ° resolution using synchrotron radiation (lambda = 0.900 A). X-ray diffraction data are collected at -173°C and processed to 1.9 A ° resolution with 98.2% completeness. The TcDHOD crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.87, b = 71.89, c = 123.27 A; DHOD–orotate complex by the sitting-drop vapour-diffusion technique using polyethylene glycol 3350 as a precipitant, to better than 1.8 A resolution, crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 67.87, b = 71.89, c = 123.27 A
by the vapour-diffusion technique using lithium sulfate as the precipitating agent, to better than 2.0 A resolution, crystals belong to space group P61, presence of two molecules in the asymmetric unit; crystallized by the vapour-diffusion technique using sitting and hanging drops (lithium sulfate as the precipitating agent). The crystals belong to space group P6(1), with unit-cell parameters a = 143.7, c = 69.8 A. X-ray diffraction data are collected to 2.0 A resolution using an in-house rotating-anode generator
hanging drop vapour diffusion method, with 30% PEG 6000, 1 mM dithiothreitol, 0.2 M sodium acetate, and 0.1 M Tris-HCl at pH 8.5
in ligand-free form and in complexes with inhibitor oxonate, physiological substrates and products of the first and second half-reactions. Ligands bind to the same active site of enzyme, consistent with one-site ping-pong Bi-Bi mechanism. The binding of ligands does not cause any significant structural changes, and both reduced and oxidized FMN cofactors are in planar conformation. Resiude C130 is well located for abstracting a proton from dihydroorotate C5 and transferring it to outside water molecules. The bound fumarate is in a twisted conformation, which induces partial charge separation. The thermodynamically favorable reduction of fumarate with reduced FMN seems to proceed in the way that its C2 accepts a proton from C130 and C3 a hydride or a hydride equivalent from reduced FMN N5
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