EC Number   |
Reference |
|---|
    2.3.1.57 | crystal structure is determined in an apo-form and in complex with its natural ligand (acetyl coenzyme A) and in complex with a product of reaction (coenzyme A) obtained by cocrystallization with spermidine |
749248 |
| 2.3.1.57 | enzyme in ligand-free form or complxed with spermine or spermidine, and/or acetyl-CoA, X-ray diffraction structure determination and analysis at 1.85-2.83 A resolution, the enzyme occurs in open and closed conformations |
736639 |
| 2.3.1.57 | hanging drop vapor diffusion method, crystal structure of PaiA in complex with CoA at 1.9A resolution, crystals belong to space group C222(1), with cell parameters of alpha = 39.9 A, beta = 135.8 A and gamma = 132.4 A |
674508 |
| 2.3.1.57 | in complex with spermidine and CoA, sitting drop vapor diffusion method, using 0.1 M Ca-acetate, 0.05 M Na-cacodylate pH 6.5, and 9% (w/v) PEG8000 |
756930 |
| 2.3.1.57 | molecular modeling of structure. Both spermidine and spermine should bind at unique position with high specificity |
718795 |
| 2.3.1.57 | precipitation with polyethylene glycol, high resolution structures of wild-type and mutant SSAT, as the free dimer and in binary and ternary complexes with CoA, acetyl-CoA, spermine, and the inhibitor N1,N11-bis-(ethyl)-norspermine |
676840 |
| 2.3.1.57 | purified enzyme, dodecameric structure in a ligand-free form in three different conformational states, open, intermediate and closed, sitting drop vapor diffusion method, for open state crystals: mixing of 400 nl of 10 mg/ml protein in 100 mM sodium chloride, 10 mM HEPES, pH 7.5, with 400 nl of reservoir solution containing 8% isopropanol and 0.1 M Tris-HCl, pH 8.5, for closed state crystals: mixing of 0.001 ml of 8.5 mg/ml protein in 500 mM sodium chloride, 5 mM 2-mercaptoethanol, 10 mM Tris-HCl, pH 8.3, with 0.001 ml of reservoir solution that contains 0.05 M ammonium sulfate, 0.1 M tri-sodium citrate and 15% polyethylene glycol 8000, and for intermediate state crystals: 0.001 ml of 8.5 mg/ml protein in 500 mM sodium chloride, 5 mM 2-mercaptoethanol, 10 mM Tris-HCl, pH 8.3, and 0.001 ml of reservoir solution containing 0.01 M calcium chloride, 20% methanol, and 0.1 M Tris-HCl, pH 8.5, 19°C, X-ray diffraction structure determination and analysis at 2.38-2.88 A reolution, molecular replacement. All structures are crystallized in C2 space group symmetry and contain six monomers in the asymmetric unit cell. Two hexamers related by crystallographic 2fold symmetry form the SpeG dodecamer. The open and intermediate states have a unique open dodecameric ring |
736641 |
| 2.3.1.57 | purified recombinant enzyme, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 40 mg/ml protein in 10 mM HEPES-KOH pH 7.5, 50 mM CoA, 50 mM spermidine, 300 mM KCl, 0.1 mM EDTA, 6 mM 2-mercaptoethanol, 10% glycerol, 10 mM PMSF, 0.02% Brij-35, with 0.001 ml of reservoir solution containing 50 mM sodium cacodylate, pH 6.5, 9% w/v PEG 8000, 0.1 M calcium acetate, and equilibration against 0.5 ml reservoir solution, 20°C, a few days, X-ray diffraction structure determination and analysis at 2.5 A resolution |
735387 |
| 2.3.1.57 | sitting drop vapor diffusion method, using 0.2 M ammonium phosphate monobasic, 0.1 M Tris, 50% (w/v) 2-methyl-2,4-pentanediol, pH 8.5 |
755723 |
| 2.3.1.57 | small angle X-ray scattering curves from two sets of a two-fold dilution series containing five sample dilutions of enzyme with and without presence of spermine |
735996 |
