Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
purified detagged recombinant enzyme in ternary complex with product D-glycerate and cofactor NADPH, sitting drop vapour diffusion method, 5.5 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 1 mM 2-mercaptoethanol, 0.2 mM NADPH, and 0.5 mm di-sodium oxalate, mixed with mother liquor, containing 15% w/v PEG 8000, 0.2 M ammonium sulfate, and 0.1 M sodium cacodylate, pH 6.5, to 0.002 ml drops, 18°C, X-ray diffraction structure determination and analysis at 2.2 A resolution; sitting-drop vapour-diffusipon method. Crystal structure at 2.2 Å resolution. There are four copies of GRHPR in the crystallographic asymmetric unit: in each homodimer, one subunit forms a ternary (enzyme/NADPH/reduced substrate) complex, and the other a binary (enzyme/NADPH) form. The spatial arrangement of the two enzyme domains is the same in binary and ternary forms
sitting drop vapor diffusion method in the presence of NAD, crystal structure analysis reveals tightly bound NADP(H) at the enzyme originating from Escherichia coli expression, which is not replaceable by NAD