EC Number |
---|
2.7.9.3 | - |
2.7.9.3 | mutant enzyme C17S in apo form, hanging drop vapor diffusion method, using 50 mM Tris-HCl (pH 8.25), 50 mM MgCl2, and 32% (w/v) PEG MME 550 |
2.7.9.3 | purified recombinant truncated mutant enzyme SPS-DELTAN, mixing of 0.001 ml of protein solution, containing 9.9 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 2 mM dithiothreitol, and 150 mM NaCl, with 0.001 ml of a reservoir solution containing 100 mM Na HEPES, pH 7.1, 50% 2-methyl-2,4-pentanediol, 200 mM ammonium phosphate, and 50 mM ammonium sulfate and equilibrating this mixture against 0.5 ml reservoir solution at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, hexameric crystal structure |
2.7.9.3 | recombinant His6-tagged enzyme, from 0.1 M trisodium citrate, pH 5.6, 17% w/v, PEG 3350 using the microbatch method, 2 months, X-ray diffraction structure determination and analysis at 3.40 A resolution |
2.7.9.3 | SPS2 free or with bound alpha/beta-methylene ATP, X-ray diffraction structure determination and analysis at 1.98-2.1 A resolution, molecular replacement |
2.7.9.3 | the crystal structures of selenophosphate synthetase 1 and of selenophosphate synthetase 1 complexed with AMPCP and K+ are solved to a resolution of 2.0 and 1.9 A, respectively |
2.7.9.3 | the recombinant full-length enzyme cannot be crystallized, but the DELTAN-LmSPS2, which lacks residues 1-69, is efficiently crystallized, from 0.2 M ammonium sulfate, 0.1 M trisodium citrate, pH 5.2, and 21% w/v PEG 4000, 3 days, X-ray diffraction structure determination and analysis at 1.88 A resolution |