EC Number   |
|---|
   3.3.2.8 | modeling of substrate 1,2-epoxymenth-8-ene into the active site of crystal structure and evaluation of the roles of residues Arg99, Tyr53 and Asn55 by QM/MM-scannedenergy mapping |
| 3.3.2.8 | mutant SZ348, sitting-drop vapor diffusion method, crystallized in 2.4 M sodium/potassium phosphate, 0.1 M Tris-HCl, pH 8.5, mixing of 0.002 ml of 16 mg/ml protein solution with 0.002 ml of reservoir solution, equilibration against the reservoir solution. The complex crystals of SZ348-CYO1 are made by soaking the crystals of SZ348 in sodium/potassium phosphate, 0.1 M Tris-HCl, pH 8.5, 10 mM of cyclopentene-1,2-epoxide, and 2.5% v/v acetonitrile for 5-10 min, at 18°C, X-ray diffraction structure determination and analysis |
| 3.3.2.8 | purified enzyme mutant H-2-H5 (E45D/L74F/T76K/M78F/N92K/L114V/I116V) and mutant H-2-H5 in complex with (S,S)-cyclohexenediol, sitting-drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 50 mM potassium phosphate buffer, pH 8.0, with 0.001 ml of reservoir solution containing 0.1 M HEPES, pH 7.5, 2% v/v PEG 400, and 2.0 M ammonium sulfate, and equilibration against reservoir solution, 20°C, the single protein crystals are soaked in 100 mM ligand solution for 1 min, X-ray diffraction structure determination and analysis, molecular replacement method using the wild-type LEH (PDB ID 1NU3) as a search model, comparison of crystal structures of wild-type and mutant enzymes |
| 3.3.2.8 | purified recombinant enzyme in apoform or in complex with inhibitor poly(ethylene glycol), 10 mg/ml protein solution is mixed with an equal volume of precipitant solution and is covered with a 1:1 mix of silicon and paraffin oils, X-ray diffraction structure determination and analysis at 1.42-1.47 A resolution |
| 3.3.2.8 | purified recombinant enzyme in apoform or in complex with inhibitor valpromide, 10 mg/ml protein solution is mixed with an equal volume of precipitant solution and is covered with a 1:1 mix of silicon and paraffin oils, X-ray diffraction structure determination and analysis at 1.16-1.26 A resolution |
| 3.3.2.8 | selenomethionine-substituted enzyme |
