EC Number   |
Reference |
|---|
    3.2.1.179 | crystallized at 20°C from a droplet containing 56% 2-methyl-2,4-pentanediol, 0.1 M NaCl, 0.1 M glycine/NaOH pH 8.2 and 0.1 M dithiothreitol using the hanging-drop vapour-diffusion method. The crystals are hexagonal and belonged to space group P6122 or P6522, with unit-cell parameters a = b = 102.8, c = 223.4 A. Diffraction data to 2.4 A are collected from a single crystal |
706951 |
| 3.2.1.179 | crystals are obtained by using hanging drop vapor diffusion and microseeding, wild-type enzyme, mutant enzyme D88N and mutant enzyme D88N in complex with beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc |
708988 |
| 3.2.1.179 | partially purified recombinnat enzyme, hanging-drop vapor-diffusion method, mixing 0.002 ml 7.5 mg/ml protein solution with 0.002 ml reservoir solution consisting of 0.1 M Tris, pH 7.75, 16% w/v PEG 4000, 21°C, X-ray diffraction structure determination and analysis at 1.6 A resolution, modelling |
752393 |
| 3.2.1.179 | purified recombinant enzyme mutants D115N and D115N/K370S, sitting drop vapor diffusion, 20 mg/ml and 40 mg/ml protein solution, respectively, is mixed with an equal volumes of reservoir solution. The reservoir solution for mutant D115N crystallization contains 1.5 M ammonium sulfate and 0.1 M Tris-HCl, pH 9.0, D115N crystals are grown at 20°C for a week. The reservoir solution for mutant D115N/K370S crystallization contains 40% ethylene glycol, 0.5 mM dithiothreitol, and 0.1 M Tris-HCl, pH 7.0, D115N/K370S is crystallized at 20°C for 2 months. X-ray diffraction structure determination and analysis at 2.00 A and 1.79 A resolution, respectively |
755323 |
| 3.2.1.179 | sitting-drop vapor duffusion method, X-ray crystallographic structure of the enzyme at 1.8 A resolution |
708980 |
| 3.2.1.179 | vapor diffusion method, demonstration of substrate recognition mechanism of the unsaturated glucuronyl hydrolase by determining the X-ray crystallographic structure of its substrate-enzyme complexes (D88N/DELTAGlcA-Glc-Pha-Glc and D99N/DELTAGlcA-GlcNAc). The tetrasaccharide-enzyme complex demonstrates that at least four subsites are present in the active pocket |
707352 |
