EC Number   |
Reference |
|---|
    2.3.1.30 | crystal structure of serine acetyltransferase (SAT) isoform 1 at 1.77 A, in complex with its substrate serine at 1.59 A and inhibitor Cys at 1.78 A resolution is reported |
719916 |
| 2.3.1.30 | crystal structure of the enzyme with its inhibitor L-cysteine |
676935 |
| 2.3.1.30 | crystals of Haemophilus influenzae O-acetylserine sulfhydrylase (EC 2.5.1.47) in complex with the C-terminal 10-residue peptide of serine acetyltransferase are prepared under silicon oil by using the sitting drop method |
662033 |
| 2.3.1.30 | hanging drop vapour diffusion method, 8-16% polyethylene glycol 1000, 10 mM Tris-HCl, pH 7.5, 2-4 weeks, room temperature, structure analysis |
486757 |
| 2.3.1.30 | purified enzyme in apoform and complexed with L-serine and CoA, hanging drop vapor diffusion method, mixing of 0.005 ml of 10-20 mg/ml protein in 10 mM Tris, pH 8.0, 50 mM NaCl, and 5 mM 2-mercaptoethanol with 0.005 ml of reservoir solution, containing 1.8 M ammonium phosphate, 100 mM imidazole, pH 8.0, and equilibration ver 0.5 ml reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.7-3.0 A resolution, method optimization |
736438 |
| 2.3.1.30 | purified His-tagged enzyme in complex with L-cysteine, mixing of 0.002 ml of 30 mg/ml protein in 20 mM Tris pH 8.0; 50 mM NaCl and 5% glycerol, with 0.0016 ml of reservoir solution with 400 nl 3% w/v trimethylamine N-oxide dehydrate additive and 25% ethylene glycol as precipitant, and equilibration against reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement using Escherichia coli CysE hexameric structure (PDB ID 1T3D) as a search model |
756960 |
| 2.3.1.30 | purified recombinant enzyme in apo state and in complex with coenzyme A, hanging drop vapour diffusion methd, mixing of 14 mg/ml protein in 50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 5% glycerol, and 5 mM 2-mercaptoethanol with reservoir solution containing 7% w/v PEG 1000, 7% w/v PEG 3350, 5% v/v MPD, 0.12 methylene glycol, 0.1 M Tris-HCl, pH 7.4, and 50 mM MgCl2, 16°C, X-ray diffraction structure determination and analysis at 1.96 A and 1.87 A resolution, respectively |
735709 |
| 2.3.1.30 | purified recombinant wild-type and mutant G52A-P55G enzymes, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml of protein in 20 mM Tris-HCl, pH 7.6, 0.2 M NaCl, 5 mM dithiothreitol, and 1 mM EDTA, with 0.001 ml of precipitant solution containing 0.1 M Tris-HCl, pH 7.5, 25% w/v PEG 4000, and 0.2 M ammonium acetate, 3 weeks, structure modeling, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution |
736358 |
| 2.3.1.30 | recombinant enzyme, crystals grew from 0.1 M MES, pH 6.6, 1ß% 2-methyl-2,3-pentanediol, 0.5 M sodium thiocyanate, 5.5 mM cysteine, and SeMet SAT (10 mg/ml) sitting drops, at 20°C within 7 days. 2.2 A crystal structure of the enzyme, which is s dimer of trimers in complex with cysteine |
659391 |
| 2.3.1.30 | vapor diffusion method. Crystal structure of Arabidopsis thaliana O-acetylserine aulfhydrylase bound with a peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase (C10 peptide) at 2.9 A resolution |
676429 |
