EC Number   |
|---|
    6.1.1.2 | - |
| 6.1.1.2 | active, truncated TrpRS lacking the N-terminal domain, sitting drop vapor diffusion at room temperature, 0.00015 ml of 24.7-32.1 mg/ml protein in 0.5 M NaCl, 25 mM HEPES, pH 7.5, 5% glycerol, and 0.025% Na-azide plus 10 mM ATP, 1 mM TCEP, 10 mM MgCl2, 2 mM L-tryptophan, is mixed with 0.00015 ml of reservoir solution containing 0.2 M MgCl2, 0.1 M Bis-Tris, pH 6.2, and 28% w/v PEG 3350, X-ray diffraction structure determination and analysis at 2.4 A resolution |
| 6.1.1.2 | catalytic fragment, hanging drop method, 0.002 ml protein solution: 8 mg/ml protein, 20 mM Tris-potassium phosphate, pH 6.8, 10 mM MgCl2, 5 mM 2-mercaptoethanol, plus equal volume of reservoir solution: 16% w/v polyethylene glycol 1500, 4% polyehylene glycol 3350, 0.2 M trisodium citrate dihydrate, pH 8.2, plus 0.0005 ml 30% 2-methyl-2,4-pentanediol, 7-10 days, 4°C, proteolytic cleavage of the enzyme into 2 fragments occurs during the crystallization process, X-ray diffraction structure determination at 2.5 A resolution using the MAD method, and analysis |
| 6.1.1.2 | crystal structure determination at 2.1 A resolution of the enzyme with a tryptophanyladenylate bound at the active site, cocrystal structure determination at 1.6 A resolution of an active fragment of the enzyme with its cognate amino acid analogue |
| 6.1.1.2 | crystal structure of drTrpRS II without ligands and in complex with ATP, hanging drop vapor diffusion method at 25°C |
| 6.1.1.2 | crystal structure of hTrpRS in complexes with Trp, tryptophanamide and ATP and tryptophanyl-AMP, respectively, are all determined at 2.4 A resolution |
| 6.1.1.2 | crystallization of native enzyme and selenomethionyl enzyme complexed with ATP, L-tryptophan and analogue indolmycin by microdialysis, formation of high-affinity or low-affinity complexes with ATP at 1 mM and 10 mM, respectively, for microclinic crystals: 0.002 ml enzyme solution, containing 4 mg/ml protein and 50% v/v glycerol, plus 2 ml well solution, 42°C, 2 M potassium phosphate, pH 6.6, 20 mM MgCl2, and 2 mM tryptophan or 1 mM ATP, for tetragonal crystals: 35°C, precipitant solution containing 1 M sodium citrate, 10 mM ATP, 10 mM MgCl2, 0.05 mM tryptophanamide, crystal growth within 1 week, X-ray diffraction structure determination at 2.3 A for the selenomethionyl-enzyme and 2.2 A for the native enzyme, structural data and analysis |
| 6.1.1.2 | crystals of native mini TrpRS are obtained by hanging-drop vapor diffusion at 4°C, crystal structure of human mini TrpRS is determined at a resolution of 2.3 A |
| 6.1.1.2 | cytosolic isoform, sitting drop vapor diffusion at room temperature, 0.0001 ml of 13.2 mg/ml protein in 0.5 M NaCl, 25 mM HEPES, pH 7.5, 5% glycerol, and 0.025% Na-azide is mixed with 0.0002 ml of reservoir solution containing 0.2 M Na-citrate, and 20% w/v PEG 3350, X-ray diffraction structure determination and analysis at 2.8 A resolution |
| 6.1.1.2 | cytosolic isoform, sitting drop vapor diffusion at room temperature, 0.0001 ml of 17.8 mg/ml protein in 0.5 M NaCl, 25 mM HEPES, pH 7.5, 5% glycerol, and 0.025% Na-azide plus 1mM tris(2-carboxyethyl)phosphine is mixed with 0.0002 ml of reservoir solution containing 0.2 M Na malonate, pH 7.0, and 20% w/v PEG 3350. triclinic crystals X-ray diffraction structure determination and analysis at 2.8 A resolution |
