EC Number |
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4.1.1.2 | - |
4.1.1.2 | purified His6-tagged enzyme mutant T165V, sitting drop vapor diffusion method, mixing of 0.0012 ml of 6 mg/mL protein in 1 mM HEPES buffer, pH 7.5, with 0.0012 ml of precipitant solution containing 10% w/v PEG 6000 and 2 M NaCl, and equilibration against well solution, 17°C, 1 week, X-ray diffraction structure determination and analysis at 2.31 A resolution |
4.1.1.2 | purified recombinant enzyme, hanging drop vapor diffusion method, 0.001 m1 of 10 mg ml protein in 50 mM Tris-HCl, pH 8.5, containing 500 mM NaCl mixed with 0.001 ml of precipitant containing 4.5% w/v PEG 2000, 100 mM Tris-HCl, pH 8.5, 100 mM glycine, 5 mM DTT, and 0.5 mM MnCl2, suspended over 1 ml of precipitant at 18 °C, crystal cryoprotection by crystallization solution containing 25% w/v glycerol, X-ray diffraction structure determination and analysis at 1.80 A resolution, modelling |
4.1.1.2 | purified recombinant His6-tagged Mn(II)-substituted W132F enzyme mutant, hanging drop vapour diffusion method, mixing of 0.002 ml of 5 mg/ml protein in 100 mM Tris-HCl, pH 8.5, and 500 mM NaCl with.0.002 ml of well solution containing 100 mM Tris-HCl, pH 8.5, 2 M NaCl, and 10% PEG 6000, 17°C, 2 months, X-ray diffraction structure determination and analysis at 1.9-2.1 A resolution |
4.1.1.2 | purified recombinant mutants R92A, DELTA162-163, S161A, and E162A, hanging-drop vapour diffusion method at 18°C, the mutants enzymes generally crystallize with 8-15% v/v PEG 8000, 0.1 M Tris, pH 8.5, and 0-15% xylitol, further method optimization for each mutant enzyme, X-ray diffraction structure determination and analysis at 2.0-3.1 A resolution, molecular modelling |
4.1.1.2 | recombinant OXDC, 3-dimensional structures in absence of formate and complexed with formate, hanging drop vapor diffusion technique, X-ray analysis |
4.1.1.2 | recombinant OxdC, hanging drop vapour diffusion method, X-ray analysis |