EC Number   |
|---|
   1.1.1.214 | homology modeling of structure and docking analysis. Structure reveals a triosephosphate isomerase barrel fold comprised of eight beta-strands and eight alpha-helices |
| 1.1.1.214 | purified enzyme in apoform and in complex with NADPH, mixing of 0.001 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution consisting of 0.1 M Tris-HCl, pH 8.1, and 23% w/v PEG 3350 at 20°C, for the enzyme-NADPH complexed crystals, the protein in 20 mM Tris-HCl, pH 8.0, and 5 mM MADPH, is mixed with 0.1 M TrisHCl, pH 7.4, and 256% w/v PEG 3350, X-ray diffraction structure determination and analysis at 1.70 A and 1.80 A resolution, respectively, molecular replacement method |
| 1.1.1.214 | purified enzyme in complex with NADPH, sitting drop vapor diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 5 mM NADPH, with 0.001 ml of reservoir solution containing 0.1 M Tris-HCl, pH 8.5, 25% w/v PEG 3350, and 0.2 M NaCl, 20°C, 2 days, X-ray diffraction structure determination and analysis at 2.20 A resolution, molecular replacement and modeling |
