EC Number   |
|---|
    3.5.3.6 | - |
| 3.5.3.6 | apo-enzyme, sitting drop vapor diffusion method, using 0.9 M trisodium citrate, 0.1M sodium cacodylate pH 6.5 |
| 3.5.3.6 | catalytically important residues are C406 and H278 |
| 3.5.3.6 | crystal structure determination and analysis of purified recombinant enzyme at 1.6 and 2.0 A resolution, respectively |
| 3.5.3.6 | crystal structure determination and analysis of purified recombinant enzyme at 2.45 A resolution, recombinant selenomethionine-labeled enzyme by sitting drop vaour diffusion method |
| 3.5.3.6 | in complex with substrate |
| 3.5.3.6 | mutants C406A, H287A, D280A, and D166A in complex with L-arginine, protein solutions containing 20 mM arginine are mixed with an equal volume of mother liquor containing 34-38% 2-methyl-2,4-pentanediol, 6.0-7.0% PEG 3350, 0.1 M Tris-HCl, pH 7.6, and 20 mM arginine, equilibration against the mother liquor reservoir, 2-8 weeks, X-ray diffraction structure determination and anaylsis at 2.3-2.9 A resolution, modeling |
| 3.5.3.6 | sitting-drop vapor-diffusion technique at 23°C, apoPAD2 crystals with increasing concentrations of calcium (0-10 mM), 16 structures are solved at eight different calcium concentrations to 1.66-1.97 A |
| 3.5.3.6 | X-ray crystallographic coordinates for the structure of the C406A ADI -L-arginine complex, overview |
