EC Number   |
Reference |
|---|
   5.1.3.31 | concentrated by ultrafiltration, sitting-drop vapour-diffusion method at 20°C |
726587 |
| 5.1.3.31 | crystal structures of the enzyme alone and in complexes with D-tagatose and D-fructose are determined at resolutions of 1.79, 2.28, and 2.06 A, respectively |
728140 |
| 5.1.3.31 | crystals are obtained by the sitting-drop method at room temperature. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 76.80, b = 94.92, c = 91.73 A , beta = 102.82° |
726603 |
| 5.1.3.31 | purified enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 10.3 mg/ml protein in 10 mM potassium phosphate, pH 7.0, with 0.001 ml of reservoir solution composed of 0.2 M ammonium acetate, 30% isopropanol, 0.1 M Tris-HCl, pH 7.5, and equilibration against 0.1 ml reservoir solution, 3-7 days, 20°C, X-ray diffraction structure determination and analysis at 2.64 A resolution, heavy metal labeleing, single isomorphous replacement with anomalous scattering, and structure molecular modeling |
746648 |
| 5.1.3.31 | recombinant enzyme mutant PcDTE_C66S in complexes with four deoxy rare sugars, 6-deoxy L-psicose, 1-deoxy 3-keto D-galactitol, 1-deoxy D-tagatose, and 1-deoxy L-tagatose, and with L-erythrulose (a sugar without groups at the 5- and 6-positions), hanging drop vapor diffusion method, mixing of 0.002 ml of 6-7 mg/ml protein in 5 mM Tris-HCl, pH 8.0, with 0.002 ml of reservoir solution containing 6.0-11.0 % w/v PEG 4000 and 100 mM CH3COONa, pH 4.6, and equilibration against 0.45 ml of reservoir solution, microgravity, X-ray diffraction structure determination and analysis at 1.59-2.3 A resolution, molecular replacement using crystal structure, PDB ID 1QUL, as a search model |
746850 |
