EC Number   |
Reference |
|---|
    6.3.3.3 | - |
1339, 1343, 1346 |
| 6.3.3.3 | at 1.65 A resolution |
1347 |
| 6.3.3.3 | crystallographic studies of complexes with substrates and a reaction intermediate |
1353 |
| 6.3.3.3 | crystals are grown from ammonium sulfate, crystals are soaked in the crystallisation-well solution plus 50 mM 6-hydroxypyrimidin-4(3H)-one for 1 hour, 6-hydroxypyrimidin-4(3H)-one is embedded in the base binding pocket of DTBS |
653958 |
| 6.3.3.3 | hanging-drop vapor diffusion, 0.005 ml of well solution containing 100 mM magnesium acetate or MgCl2, 9-11% polyethylene glycol 8000 and 100 mM cacodylate, pH 6.5 are mixed with 0.002 ml protein solution containing 30 mg/ml DTBS, crystals grow within a week at 20°C, crystals of DTBS complexed with diaminopelargonic acid-MgADP-AlF3 and with dethiobiotin-MgADP-phosphate, crystals diffract to 1.8 A |
653820 |
| 6.3.3.3 | hanging-drop vapor diffusion, precipitant polyethylene glycol 8000, 100 mM cacodylate, pH 6.5, 200 mM magnesium acetate, crystals diffract to 0.97 A |
649107 |
| 6.3.3.3 | in complex with CTP, to 2.3 A resolution. The nucleoside base is stabilized in its pocket through hydrogen-bonding interactions with the protein backbone, rather than amino acid side chains. DTBS could utilise ATP, CTP, GTP, ITP, TTP, or UTP with similar Km and kcat values |
746545 |
| 6.3.3.3 | in complexes with the substrate 7,8-diaminopelargonic acid or ADP and the product dethiobiotin, up to 1.85 A resolution. |
714208 |
| 6.3.3.3 | X-ray crystallographic studies of the mutant enzymes S41A, S41C, K37Q, and K37L, show that the crystals are essentially isomorphous to that of the wild-type DTBS |
1350 |
