EC Number   |
|---|
   2.4.2.2 | crystal structure of the enzyme with the substrate analog, pseudouridine, in its active site is solved to 2.1 A |
| 2.4.2.2 | crystallized at 18°C using the oil-microbatch method with PEG 4000 as a precipitant. A native data set is collected to 1.8 A resolution using synchrotron radiation. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 58.83, b = 76.23, c = 103.86 A, beta = 91.3 |
| 2.4.2.2 | crystals: monoclinic with dimensions of 0.13 * 0.13 * 0.07 mm, X-ray diffraction to 1.8 Å using synchrotron radiation at -173°C, belong to space group P2(1), asymmetric unit contains dimer with local pseudo-twofold symmetry, unit-cell parameters: a: 58.83, b: 76.23, c: 103.86, beta: 91.3°, oil-microbatch method: 1 week at 18°C, drop: 0.5 microlitre precipitant solution (27.5% (w/v) PEG 4000 in 100 mM HEPES-NaOH pH 7.5, 10 mM CaCl2) + 0.5 microlitre protein solution (21.7 mg/ml in 20 mM Tris-HCl pH8, 200 NaCl) |
| 2.4.2.2 | hanging-drop vapor diffusion method, crystals of the protein-inhibitor complex with the substrate analog pseudouridine |
| 2.4.2.2 | in complex with the products, ribose 1-phosphate and uracil, at 1.8 A resolution. The biological unit is a hexamer with an alpha/beta monomeric fold. Residue His169 structurally aligns with Arg168 of the Escherichia coli uridine phosphorylase structure. A second active site residue, Lys162, is not present in previously determined uridine phosphorylase structures and interacts with O2 of uracil |
| 2.4.2.2 | purified enzyme in complex with imidazole and sulfate, sitting drop vapour diffusion, mixing of 0.002 ml of 16 mg/ml protein in 20 mM Tris-HCl, 500 mM KCl with 0.002 ml of reservoir solution containing 0.2 M ammonium acetate, 0.1 M bis-Tris, pH 5.5, X-ray diffraction structure determination and analysis at 1.88 A resolution |
