EC Number   |
|---|
    1.1.1.79 | analysis of the three-dimensional crystal structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR |
| 1.1.1.79 | enzyme with NADP+ plus sulfate, sitting drop vapor diffusion method, using 0.1 M Bis-Tris pH 5.5, 25% (w/v) PEG 3350, 0.2 M ammonium sulfate. Enzyme with NADPH plus oxalate, sitting drop vapor diffusion method, using 0.2 M ammonium citrate tribasic pH 7.0, 20% (w/v) PEG 3350. Apo enzyme form, sitting drop vapor diffusion method, using 0.1 M sodium citrate, pH 5.6, 20% (v/v) 2-propanol, 20% (w/v) PEG 4000 |
| 1.1.1.79 | purified apo-enzyme, sitting drop vapor diffusion method, mixing of 0.002 ml of protein solution with 0.002 ml of reservoir solution containing 0.2 M calcium acetate hydrate, 20% PEG 3350, pH 6.5, 20°C, 6 weeks, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using a previously unrecognized member of the beta-HAD family, cytokine-like nuclear factor, structure |
| 1.1.1.79 | 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 |
| 1.1.1.79 | purified recombinant enzyme, sitting drop vapour diffusion method, the reservoir solution contains 0.1 M MES buffer, pH 6.5, 0.01 M cobalt (II) chloride, and 1.8 M ammonium sulfate, 20°C, X-ray diffraction structure determination and analysis at 1.75 A resolution |
| 1.1.1.79 | purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, hanging drop vapour diffusion method, from a mother liquor containing 100 mM sodium acetate, pH 5.2, 15% PEG 400, and 100 mM NaCl, 20°C, X-ray diffraction structure determination and analysis at 1.4-2.0 A resolution |
| 1.1.1.79 | purified thermostable GRHPR in a binary complex with glyoxylate, and in a ternary complex with D-glycerate and NADPH, sitting drop vapour diffusion method, mixing of 0.0015 ml of 10 mg/ml protein solution with 0.0015 ml of mother liquor containing 1.7 malonate, pH 7.0, 20°C, X-ray diffraction structure determination and analysis at 1.4 A-2.0 A resolution, molecular replacement using the three-dimensional structure of the monomer of Pyrococcus horikoshii PhoGRHPR, PDB ID 2DBR |
| 1.1.1.79 | 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 |
| 1.1.1.79 | 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 |
