EC Number   |
Reference |
|---|
   6.5.1.3 | 2.2 A resolution, crystal structure of a complete RNA ligase, Rnl1, in complex with adenosine 5'-(alpha,beta-methylenetriphosphate) |
674568 |
| 6.5.1.3 | 2.6 A crystal structure |
677128 |
| 6.5.1.3 | crystal structure of the catalytic domain of TbREL1 at 1.2 A resolution, in complex with ATP and magnesium.The magnesium ion interacts with the beta and gamma-phosphate groups and is almost perfectly octahedrally coordinated by six phosphate and water oxygen atoms. Sitting-drop, vapor-diffusion with 100 mM HEPES, 100 mM Mg2+ and 35% (w/v) PEG3350 at pH 7.0. The crystal belongs to space group P2(1), with cell dimensions of a = 44.9 A, b = 58.6 A, c = 53.0 A and beta = 100.2°, and one molecule in the asymmetric unit |
662636 |
| 6.5.1.3 | crystal structure of the ligase domain with AMP bound at the active site, space group P2(1)2(1)2, a = 57.72 A, b = 89.89 A, c = 47.74 A |
653915 |
| 6.5.1.3 | hanging drop vapor diffusion method, using 0.1 M HEPES pH 6.5, 30% (w/v) PEG6000 |
749172 |
| 6.5.1.3 | hanging-drop vapor diffusion. Crystal structures of: 1. Covalent Rnl2-AMP intermediate, 2. Rnl2 bound to an adenylylated nicked duplex, captured immediately following reaction step 2, 3. Rnl2 at an adenylylated nick in a state poised for step 3. These structures illuminate the stereochemistry of nucleotidyl transfer and reveal how remodeling of active-site contacts and conformational changes propel the ligation reaction forward |
672949 |
| 6.5.1.3 | in complex with ATP or AMP, hanging drop vapor diffusion method, using 0.1 MTris-HCl (pH 8.5), 0.2 M lithium sulfate and 40% (w/v) PEG400 |
748784 |
| 6.5.1.3 | virtual screen of REL1 crystal structure for inhibitors |
694881 |
