EC Number   |
|---|
   3.1.4.41 | hanging drop vapor diffusion method. crystal structure determined ar 1.75 A resolution using the quick cryo-soaking technique. The enzyme folds as an (alpha/beta)8 barrel, the interfacial and catalytic sites encompass hydrophobic loops and a negatively charged surface |
| 3.1.4.41 | hanging-drop vapour-diffusion method. Crystal structure of the sulfate free enzyme determined at 1.85 A resolution. The metal ion is tetrahedrally coordinated instead of the trigonal-bipyramidal coordination observed in the sulfate bound form |
| 3.1.4.41 | purified PLD, sitting drop vapor diffusion method, 0.002 ml of 17 mg/ml protein solution is mixed with 0.002 ml of reservoir solution containing 0.1 M Tris-HCl, pH 7.5, 40% v/v PEG 200, and equilibration over 1 ml reservoir solution, 18°C, X-ray diffraction structure determination and analysis at 1.7 A resolution |
| 3.1.4.41 | purified recombinant enzyme, hanging drop vapour diffusion method, mixxing of 0.001 ml of 15 mg/ml protein in phosphate buffer, pH 7.0, with 0.001 ml reservoir solution containing 0.1 M Tris-HCl, pH 8.2, 22% PEG 10000, equilibration against 0.5 ml reservoir solution, 18°C, X-ray diffraction structure determination and anaysis at 2.6 A resolution |
| 3.1.4.41 | purified recombinant wild-type and H12A mutant enzymes, 0.002 ml of protein solution containing 17 mg/ml wild type enzyme and 9 mg/ml H12A mutant, respectively, are mixed with 0.002 ml of reservoir solution containing 0.1 M Tris-HCl, pH 7.5, 40% v/v PEG 200 for the wild-type enzyme, and 0.1 M Tris-HCl, pH 7.5 and 35% v/v PEG 200 for the H12A mutant, equilibration over 1 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.95 and 1.6 A resolution, respectively |
