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purified recombinant detagged enzyme, hanging drop vapor diffusion method, mixing of 0.0003 ml 6 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 200 mM NaCl, and 10% glycerol, with 0.0003 ml of reservoir solution containing 1.2 M sodium citrate tribasic dihydrate, pH 7.0, 20°C, method optimization, X-ray diffraction structure determination and analysis
tetrameric enzyme, hanging drop vapour diffusion method, 15°C, 17 mg/ml protein in 10 mM potassium phosphate buffer, pH 7.0, equilibration of the 0.002 ml protein drop against 500 ml reservoir solution consisting of 1.4 M ammonium sulfate, 5% v/v MPD, 2 mM NAD+, 50 mM sodium citrate buffer, pH 5.5, 2-3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution
purified recombinant enzyme in apoform and in complex with NAD+, sitting drop vapor diffusion method, mixing 500 nl of 10 mg/ml protein with an equal volume of mother liquor and equilibration against 0.1 ml of the crystallization solution containing 100 mM Tris-HCl, pH 8.2, 22.5% w/v PEG4000, and 200 mM magnesium chloride, at 10°C, 5 days. NAD-bound form crystals are obtained by soaking the apo-form crystal with a 001 ml crystallization reservoir containing 2 mM NAD+ molecule for about 30 min immediately prior X-ray diffraction, X-ray diffraction structure determination and analysis at 1.80-2.36 A resolution, molecular replacement and modelling, overview