EC Number   |
|---|
   5.4.2.6 | beta-PGM is transferred to 1 mM HEPES, pH 7.5, 10 mM MgCl2 and 0.1 mM dithiothreitol, final beta-PGM concentration at 15 mg/ml, crystals are obtained from either 150 mM ammonium acetate, 100 mM trisodium citrate dihydrate, pH 4.5, 25% polyethylene glycol 4000 or 100 mM ammonium fluoride, 16% polyethylene glycol 3350 by hanging-drop vapor diffusion, crystals of selenium methionyl-substituted beta-PGM diffract to 2.3 A |
| 5.4.2.6 | both in complex with inhibitor alpha-D-galactose 1-phosphate or substrate beta-D-glucose 1-phosphate |
| 5.4.2.6 | characterization of the solution structure of the MgF3- complex bound to the enzyme active site |
| 5.4.2.6 | crystals of phosphorylated native beta-PGM are grown at pH 7.5 in the presence of 5 M Mg2+ using the vapor-diffusion method with hanging drop geometry, 100 mM ammonium fluoride and 16% polyethylene glycol 3350 are used as precipitating agents, crystals diffrakt to 2.3 A |
| 5.4.2.6 | in complex with alpha-fluorophosphonates, sitting drop vapor diffusion method, using 27-32% (w/v) PEG 4000, and 50-75 mM magnesium acetate |
| 5.4.2.6 | in complex with Mg2+ |
| 5.4.2.6 | purified recombinant enzyme in complex with transition-state analogue fluoromagnesate and glucose 6-phosphate or ground-state analogue fluoroaluminate and glucose 6-phosphate, sitting drop vapour diffusion method, mixing of 15 mg/mL 50 mM K+ HEPES, pH 7.2, 5 mM MgCl2, 1 mM azide, 0.1 mM DTT, 10 mM NH4F, and 10 mM BeCl2 1:1 with the precipitant containing 26-30% w/v PEG 4000, 200 mM Na acetate, and 100 mM Tris, pH 7.5, X-ray diffraction structure determination and analysis at 1.65 A resolution, molecular replacement |
| 5.4.2.6 | sitting drop vapor diffusion method, using 0.1 M trisodium citrate pH 5.0 containing 1.8 M ammonium sulfate |
