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EC Number Crystallization (Commentary)
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B52crystallized under a reservoir solution condition of 0.2 M ammonium acetate, 0.1 M HEPES pH 8.5 and 24% (w/v) PEG3350
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B52purified recombinant His-tagged enzyme, enzyme AtQR and 2 mM NADH are crystallized from a reservoir solution containing of 0.2 M ammonium acetate, 0.1 M HEPES, pH 8.5, and 24% w/v PEG 3350, X-ray diffraction structure determination and analysis at 1.72 A resolution. Three NADH-bound protomers and one NADH-free protomer form a tetrameric structure in an asymmetric unit of crystals. NADH not only acts as a proton donor, but also contributes to the stability of the alpha7 helix. Molecular replacement using structure of meso-2,3-butanediol dehydrogenase, PDB ID 1GEG, from Klebsiella pneumoniae as template
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B52sitting-drop vapour-diffusion method at 20°C. Crystals are obtained using a reservoir solution containing PEG 3350 as a precipitant. X-ray diffraction data are collected to 1.72 A resolution. The crystal belongs to space group P2(1), with unit-cell parameters a = 62.0, b = 126.4, c = 62.0 A, beta = 110.5, and is suggested to contain four molecules in the asymmetric unit
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