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Results 1 - 8 of 8
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.1crystallization data of mutant D402N in complex with 1-nitrohexane or 1-nitrooctane show the presence of substrate in the binding site. The aliphatic chain of the substrate extends into a tunnel leading to the enzyme surface. The oxygens of the substrate nitro group interact both with amino acid residues and with the 2'-hydroxyl of the FAD. The structure of wild-type enzyme trapped with cyanide during oxidation of 1-nitrohexane shows the presence of the modified flavin. A continuous hydrogen bond network connects the nitrogen of the CN-hexyl-FAD through the FAD 2'-hydroxyl to a chain of water molecules extending to the protein surface. Data for mutant S276A in complex with nitrohexane
Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.1hanging drop vapour diffusion method
Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.1hexagonal rod-shaped crystals of R409K and D402E NAO were obtained using hanging drop vapor-diffusion methods
Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.1mutant enzyme H183S in complex with nitroethane and FMN, hanging drop vapor diffusion method, using 0.2 M ammonium fluoride, 20% (w/v) polyethylene glycol 3350
Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.1native and a selenomethionine-substituted enzyme, to 1.9 A resolution. Primitive orthorhombic space group P21, with unit-cell parameters a = 70.06, b = 55.43, c = 87.74 A, beta = 96.56° for native NAO and a = 69.89, b = 54.83, c = 88.20 A, beta = 95.79° for selenomethionine-substituted enzyme
Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.1purified recombinant wild-type enzyme, crystallization of the native enzyme in 2 different crystal forms and of the selenomethionine-labeled enzyme in a third one, hanging drop vapour diffusion method, sodium cacodylate buffer, pH 7.5, containing spermidine hydrochloride, and PEG 4000 at varying concentrations for all 3 mixtures, crystal form 2 requires addition of 1,6-hexanediol at 8% w/v, crystal form 3 requires DTT at 10 mM, 4°C, 10-14 days, X-ray diffraction structure determinations and analysis at 3.2-2.0 A resolution or below, three-wavelength MAD data
Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.1vapor diffusion method, using 2.5 M magnesium sulfate, 0.1 M 2-(N-morpholino) ethanesulfonic acid buffer, pH 6.0, and 18% (v/v) glycerol
Display the word mapDisplay the reaction diagram Show all sequences 1.7.3.1wild-type and mutant H179D. Enzyme consists of two domains, a TIM barrel domain bound to FMN and C-terminal domain with a alpha-alpha-alpha-beta-alpha-beta-alpha fold. It shows the typical function as nitroalkane oxidase but its structure is similar to that of 2-nitropropane dioxygenase
Results 1 - 8 of 8