EC Number   |
|---|
    2.4.2.17 | purified recombinant wild-type and selenomethionine-labeled enzyme complex, the latter additionally by microseeding, hanging drop vapour diffusion method, 0.002 ml well solution containing 15-25% v/v PEG 400, 0.1 M Tris-HCl, pH 7.5, 0.2 M MgCl2, mixed with equal volume of protein solution containing 10-16 mg/ml protein, 10 mM ATP, or 10 mM N-1-methyl-ATP and 5 mM 5-phospho-alpha-D-ribose 1-diphosphate, crystal growth is dependent on ATP or N-1-methyl-ATP, derivatization with 2.5 mM sodium tungstate dihydrate, cryoprotection with 17-18% glycerol, X-ray diffraction structure determination and analysis at 2.9-3.2 A resolution |
| 2.4.2.17 | purified recombinant wild-type and selenomethionine-labeled subunits HisGs and HisZ separately, in a binary complex with histidine, sitting drop vapour diffusion method, 0.002 ml of 8 mg/ml protein mixed with 0.002 ml reservoir solution containing 22.5% w/v methyl-2,4-pentanediol, 0.2 M phosphate/citrate buffer, pH 4.2, 2 days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modeling |
| 2.4.2.17 | truncated long-form enzyme devoid of its regulatory domain as apoenzyme and in complex with ATP, 5-phospho-alpha-D-ribose 1-diphosphate or 1-(5-phospho-beta-D-ribosyl)-ATP, hanging drop vapor diffusion method, using 1 M sodium acetate, 10 mM ZnCl2, and 7-10% (w/v) PEG 6000 (pH 5.0) |
| 2.4.2.17 | vapour diffusion method, trigonal prisms are obtained using 1.3 M sodium tartrate, 50-200 mM magnesium chloride, 100 mM citrate buffer pH 5.6 and enzyme in the presence of 2 mM AMP, round shaped crystals are obtained with 1.36-1.44 M ammonium sulfate, 0-0.3 M sodium chloride, 100 mM HEPES buffer pH 7.5 and enzyme in the presence of 2 mM AMP |
