EC Number   |
Reference |
|---|
    1.1.1.3 | - |
246396 |
| 1.1.1.3 | 10 mg/ml purified recombinant enzyme, in TAPS, pH 8.5, in complex with inhibitor 4,4'-thiobis[2-(1-methylethyl)-phenol] in a molar ratio of 1:1, precipitant solution contains either 0.1 CHES, pH 9.5, 35% PEG 600 or 0.1 M CHES, pH 8.5, 40% PEG 400, and 0.2 M NaCl, 0.005 ml protein complex solution are equilibrated against 0.7 ml of precipitant solution using sitting drop technique, 3 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, modeling |
654955 |
| 1.1.1.3 | for the purified ligand-free recombinant wild-type enzyme: sitting drop vapor diffusion method, mixing of 0.001 ml of 12.0 mg/ml protein solution with an equal volume of mother liquor composed of 0.1 M potassium phosphate, pH 6.2, and 20% MPD, 2 days, 20°C, for the homoserine-bound K57A mutant enzyme: sitting drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein solution containing 1 mM homoserine with 0.002 ml of mother liquor containing 16% polyethylene glycol monomethyl ether 2000 and 0.1 M citrate buffer, pH 6.5, 7 days, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement and modelling |
741408 |
| 1.1.1.3 | purified enzyme StHSD complexed with cysteine and NAD+, hanging drop vapour diffusion method, mixing of 0.002 ml of 5 mg/ml protein solution with 0.002 ml of reservoir solution containing 23% w/v PEG 3350, 0.2 M di-ammonium tartrate, 0.001 ml of 20 mM NAD+, and 0.001 ml of 100 mM cysteine, and equilibration against 0.1 ml of reservoir solution, 12°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using the StHSD structure (PDB ID 4YDR) as an initial phasing model |
762453 |
| 1.1.1.3 | purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, hanging drop and sitting drop methods of vapour diffusion, 8 mg/ml protein solution is mixed with reservoir solution, different conditions involving addition of 0.2 M magnesium acetate and PEG 3350 or 8000, and 3.5% glycerol, overview. X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution |
739804 |
| 1.1.1.3 | purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution |
739791 |
| 1.1.1.3 | purified recombinant enzyme in oxidized and in reduced form, hanging drop vapor diffusion method, for the oxidized form: mixing of 0.0015 ml of 5.9 mg/ml protein solution with 0.0015 ml of reservoir solution, pH 4.1, containing 9.5% w/v PEG 3350, 19% w/v PEG 400, 0.19 M magnesium chloride, and 2.5% DMSO, for the reduced form: soaking of the oxidized enzyme crystals in a solution consisting of 0.003 ml of reservoir solution and 0.001 ml of 200 mM DTT for 60 min prior to the first diffraction data collection, 12°C, X-ray diffraction structure determmination and analysis at 1.60-1.83 A resolution, molecular replacement and modelling |
739972 |
| 1.1.1.3 | purified wild-type homoserine dehydrogenase in apoform, complexed with L-homoserine and NADPH in a closed form, and enzyme mutants K99A and K195A complexed with L-Hse and NADP+, hanging-drop vapour-diffusion method, mixing of 0.002 ml of 5 mg/ml protein in 5 mM Tris-HCl, pH 7.5, and in case of the ligand complex forms 15 mM of each ligand, with 0.002 ml of reservoir solution containing 3.3-4.0 M sodium formate and 50 mM CAPS, pH 10.0, X-ray diffraction structure determination and analysis at 1.83 A, 2.00 A, 1.87 A, and 1.93 A resolution, respectively, molecular replacement method using the TtHSDx02L-Hse structure (PDB ID 5XDF) as the search model |
761404 |
