EC Number   |
|---|
    2.1.3.2 | - |
| 2.1.3.2 | 3 catalytic and 3 regulatory subunits per asymmetric unit |
| 2.1.3.2 | 50 mM Tis-HCl, pH 8.1, 70% ammonium sulfate |
| 2.1.3.2 | approx. 30% ammonium sulfate, crystals appear after about 2 weeks at 4°C |
| 2.1.3.2 | aspartate carbamoyltransferase in complex with its allosteric activator CTP |
| 2.1.3.2 | ATCase locked in the R quaternary structure by specific introduction of disulfide bonds bound to the final product molecule phosphate, 10 mg/ml protein solution is dialyzed against a solution of 100 mM potassium dihydrogen phosphate and 3 mM sodium azide, pH 5.9, 1 week, X-ray diffraction structure determination and analysis at 2.85 A resolution, molecular replacement |
| 2.1.3.2 | bound to N-phosphonacetyl-L-aspartate, citrate or phosphate, crystalline R-state P212121 |
| 2.1.3.2 | catalytic chain in the presence of the regulatory chain in the hexagonal space group P6322, with one monomer per asymmetric unit, sitting drop vapor diffusion method, mixing of 0.0013 protein-ligand solution, containing 11 mg/ml protein in 50 mM Tris, pH 8.3, 150 mM NaCl, 2 mM BME, 0.05 mM zinc acetate, with 0.001 ml of reservoir solution containing 2.0 M ammonium sulfate, 0.2 M potassium sodium tartrate tetrahydrate, 0.1 M sodium citrate tribasic dihydrate, pH 5.6, or 2.0 M ammonium sulfate, 0.2 M potassium sodium tartrate tetrahydrate, 0.1 M Tris-HCl, pH 7.5, 22°C, X-ray diffraction structure determination and analysis at 2.50 A resolution, molecular replacement |
| 2.1.3.2 | cocrystallization of catalytic subunit with N-(phosphonoacetyl)-L-aspartate by vapor diffusion, crystals grow from 0.005 ml of 100 mM Tris-HCl, pH 6.8, 20 mM calcium acetate, 5.8% polyethylene glycol 8000 and 0.005 ml of catalytic subunit in 10 mM Tris-HCl, pH 7.5, 1 mM 2-mercaptoethanol and 2 mM N-(phosphonoacetyl)-L-aspartate |
| 2.1.3.2 | complex of aspartate transcarbamoylase and dihydroorotase |
