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Results 1 - 7 of 7
EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.18-
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.18crystallized from ammonium sulfate solutions in a form suitable for X-ray diffraction analysis. Crystals are grown by the vapour-diffusion technique using the sitting-drop method. X-ray diffraction studies show that the crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 with a = b = 114.3 and c = 276.0 A. The crystals diffract to at least 2.4 A resolution
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.18purified native enzyme, hanging drop vapor diffusion method, mixing of 0.001-0.002 ml of 8 mg/ml protein solution with 0.0005-0.001 ml of reservoir solution containing 0.1 M sodium chloride, 0.01 M Tris-HCl, pH 5.5, and 25% PEG 3350 leading to monoclinic crystals, or 0.15 M potassium rhodanide, 0.01 M Tris, pH 7.5, and 19% PEG 3350 leading to hexagonal crystals, both at a temperature of 18°C, X-ray diffraction structure determination and analysis at 2.26 A resolution, molecular replacement and modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.18sitting drop vapour diffusion method, two crystal forms are obtained, one hexagonal form using ammonium phosphate as precipitant (form 1) and a second cubic vanadium bound form (form 2). The best crystals of the cubic form 2 containing vanadate are only obtained with the wild type enzyme. The optimised conditions use an initial protein concentration of 18 mg/ml in 50 mM Tris-H2SO4, 0.4 M KBr, 1 mM Na3VO4, 20% (w/v) polyethylene glycol 6000. For the wild type enzyme crystals grown in form 2, a mother liquor substituting the precipitant with 25% polyethylene glycol 400 and 25% polyethylene glycol 6000 is used
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.18structure of the enzyme is solved by single isomorphous replacement anomalous scattering X-ray crystallography at 2.0 A resolution. Crystals of the holoenzyme and the apoenzyme are obtained from 2.1 M ammonium sulfate solutions buffered at pH 8.3 and diffract to 2.4 A resolution. The crystals are stable in the X-ray beam for more than one week. They belong to the tetragonal system, space group P4(3)2(1)2, with lattice constants a ?= 114.3 A,? c = 276.0 A
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.18the crystals exhibit a teardrop morphology and are grown from 2 M ammonium dihydrogen phosphate pH and diffract to beyond 1.7 A resolution. They are in tetragonal space group P4222 with unit-cell dimensions of a = b = 201.9 A, c = 178.19 A, alpha = beta = gamma = 90°
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.18the hanging-drop vapor diffusion method
Results 1 - 7 of 7