EC Number   |
|---|
    3.2.2.5 | C-terminal glycohydrolase domain of SPN (residues 191-451) in complex with IFS, vapor diffusion method, using 20%-25% (w/v) PEG 8K and 100 mM Tris-HCl (pH 8.0), at 22°C |
| 3.2.2.5 | CD38 in complex with ribosyl-2'-fluoro-deoxy-adenosine diphosphate or arabinosyl-2'-fluoro-deoxy-adenosine diphosphate ribose, soaking crystals in a solution containing either 5.2 mM inhibitor, and 100 mM MES, pH 6.0, 15% PEG 4000, and 30% glycerol, X-ray diffraction structure determination and analysis at 1.75-2.0 A resolution |
| 3.2.2.5 | in complex with effector Tni2, to 1.7 A resolution |
| 3.2.2.5 | purified recombinant selenomethionine-labeled enzyme C-terminal domain (residues 193-451) in complex with the full-length inhibitor IFS, sitting drop vapor-diffusion method, mixing of 0.001 ml of protein solution with 0.001 ml of reservoir solution of 20% w/v tacsimate, pH 4.0, and 20% w/v PEG 3350, 22°C, X-ray diffraction structure determination and analysis at 1.70 A resolution, single-wavelength anomalous diffraction, modelling |
| 3.2.2.5 | purified recombinant wild-type and mutant enzymes, mixing of 0.001 ml of protein sample with 0.001 ml of precipitant solution containing 0.1 M imidazole, pH 7.5, and 12-24% PEG 4000, X-ray diffraction structure determination and analysis at 1.75-2.18 A resolution |
| 3.2.2.5 | to 1.4 A resolution, in complex with binding protein Tsi6 |
| 3.2.2.5 | wild-type and mutant E226Q in complex with cyclic ADP-ribose at 1.5 A resolution, with cyclic GDP-ribose at 1.68 A, and with NGD+ at 2.1A. Binding of cyclic ADP-ribose or cyclic GDP-ribose induce structural changes in the dipeptide E146D147 of 2.7 A. Resiudue E226 is critical in catalysis and in positioning of cyclic ADP-ribose |
| 3.2.2.5 | wild-type and mutant E226Q in complex with inhibitor N1-cyclic inosine diphosphate ribose at 1.7 and 1.176 A resolution, respectively |
| 3.2.2.5 | wild-type and mutant E226Q in complex with NAD+, NGD+, or GDP-ribose. The reaction intermediate is stabilized by polar interactions with the catalytic residue E226 rather than by a covalent linkage |
