    1.1.1.42 | 20 mg/ml purified recombinant wild-type and selenomethionine enzyme, complexed with Mn2+ and isocitrate, 4°C, hanging drop vapour diffusion method, for the wild-type enzyme: 0.002 ml of enzyme solution containing 0.1 M triethanolamine chloride, pH 7.7, 0.15 M Na2SO4, 8 mM DL-isocitrate, 4 mM MnSO4, plus equal volume of 20% PEG 6000, 3% glycerol, against 0.75 ml reservoir solution containing 0.1 M triethanolamine chloride, pH 7.7, 0.15 M Na2SO4, 8 mM DL-isocitrate, 4 mM MnSO4, and 40% w/v xylitol, for the selenomethionine enzyme: 0.002 ml of enzyme solution containing 0.1 M triethanolamine chloride, pH 7.7, 0.15 M Na2SO4, 8 mM DL-isocitrate, plus equal volume of 18% PEG 6000, 3% glycerol, against 0.75 ml reservoir solution containing 0.1 M triethanolamine chloride, pH 7.7, 0.15 M Na2SO4, and 18% PEG 6000, 7-10 days, X-ray diffraction structure determination and analysis at 2.7 A resolution, modeling |
| 1.1.1.42 | crystal structures of Saccharomyces cerevesiae mitochondrial NADP-IDH Idp1p in binary complexes with coenzyme NADP+, or substrate isocitrate, or product 2-oxoglutarate, and in a quaternary complex with NADPH, 2-oxoglutarate, and Ca2+, which represent different enzymatic states during the catalytic reaction. Crystallization is carried out at 20°C using the hanging-drop vapor diffusion method |
