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enzyme in complex with substrate urate and inhibitor cyanide, X-ray diffraction structure determination and analysis
ligand-free Uox crystallized with NH4Cl and 15% (w/v) PEG 8000, ligand-free Uox crystallized in water with 10% (w/v) PEG 8000, ligand-free Uox crystallized with NaCl and 15% (w/v) PEG 8000, ligand-free Uox crystallized with (NH4)2SO4 and 15% (w/v) PEG 8000, ligand-free Uox crystallized with NaCl and 8% PEG 8000, ligand-free Uox crystallized with KCl and 10% (w/v) PEG 8000, and Uox complexed with 8-azaxanthine and crystallized with NaCl and 10% (w/v) PEG 8000, in 50 mM Tris buffer pH 8.0
quantum mechanical/molecular mechanical calculations based on PDB entry 4N9M. The oxidation consists of chemical transformation from 8-hydroxyxythine to an anionic radical via a proton transfer along with an electron transfer, proton transfer to the O2- anion (radical), diradical recombination to form a peroxo intermediate, and dissociation of H2O2 to generate the dehydrourate. Hydration is initiated by the nucleophilic attack of a water molecule on dehydrourate, along with a concerted proton transfer through residue Thr69 in the catalytic site. Hydration is the rate-determining step
recombinant enzyme in complex with inhibitor 8-azaxanthine in presence of O2 or Cl-, batch technique at room temperature, 10-15 mg/ml protein with an excess of 0.5-2 mg/ml of 8-azaxanthin in 50 mM Tris/HCl, pH 8.5, in the presence of 5-8% w/v PEG 8000 and 0.05 M NaCl, 24-48 h, X-ray diffraction structure determination and analysis at 1.6-1.7 A resolution
sitting drop vapour diffusion method
crystallization of large proteins in the presence of polyethylene glycol
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crystals of about a few tens of micrometres in size, which is nucleated previously in crystallization batch containing 5% PEG 8000, 100 mM NaCl, 8 mg/ml uox-substrate complex and 100 mM Tris-HCl pH 8.5, are used as seeds and their size and quality are further improved using a temperature-control device, large crystals of Uox, co-crystallized with its substrates analogues 8-azaxanthine, 9-methyluric acid or the natural substrate in the presence of cyanide (0.5-2 mg/ml), and soaks with the natural substrate in the absence of cyanide, diffracting to high resolutions are obtained, in the presence of different inhibitors, the crystal form of Uox has a body-centred orthorhombic symmetry and one of the largest primitive unit-cell volumes (a: 80 A, b: 96 A, c: 106 A)
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hanging drop vapour diffusion method
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sitting drop vapour diffusion method using buffered D2O
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sitting-drop vapour-diffusion method at room temperature
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sitting-drop vapour-difusion method. Four different crystal forms of Uox are analyzed. In the presence of uracil and 5,6-diaminouracil crystals usually belong to the trigonal space group P3(1)21, the asymmetric unit of which contains one tetramer of Uox. Chemical oxidation of 5,6-diaminouracil within the protein may occur, leading to the canonical (I222) packing with one subunit per asymmetric unit. Coexistence of two crystal forms, P2(1) with two tetramers per asymmetric unit and I222, is found in the same crystallization drop containing another inhibitor, guanine. A fourth form, P2(1)2(1)2 with one tetramer per asymmetric unit, results in the presence of cymelarsan, an additive
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