EC Number   |
|---|
    2.4.2.8 | analysis of crystal structure |
| 2.4.2.8 | apo-form and in complex with GMP, sitting drop vapor diffusion method, using 0.2 M trimethylamine N-oxide dehydrate, 0.1 M Tris pH 8.5, 20% (w/v) polyethylene glycol monomethyl ether 2000 |
| 2.4.2.8 | crystallization and X-ray structure determination and analysis, 1 molecule of GMP bound per dimer |
| 2.4.2.8 | crystallization in complex with GMP and IMP, structure analysis |
| 2.4.2.8 | enzyme in complex with 2-(phosphonoethoxy)ethyl guanine, 2-(phosphonoethoxy)ethyl hypoxanthine, and (R,S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine, hanging drop vapor diffusion method, mixing of equal volumes of well solution, containing 0.1 M citrate pH 5.5, 10% isopropyl alcohol and 29% PEG 4000, and protein inhibitor complex with 17 mg/ml prtoein, and 3.3 mM for 2-(phosphonoethoxy)ethyl guanine, 3.9 mM (R,S)-9-[3-hydroxy-2-(phosphonomethoxy)propyl]guanine, and 3.0 mM for 2-(phosphonoethoxy)ethyl hypoxanthine, X-ray diffraction structure determination and analysis at 2.6-2.78 A resolution |
| 2.4.2.8 | enzyme in complex with inhibitors (2-[(2,3-dihydroxypropyl)[2-(6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]amino]ethyl)phosphonic acid, 9-[(N-phosphonoethyl-N-phosphonomethyl)-2-aminoethyl]-hypoxanthine, 9-[(N-phosphonoethyl-N-phosphonoethoxyethyl)-2-aminoethyl]-hypoxanthine, (2-[[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl][2-(2-phosphonoethoxy)ethyl]amino]ethyl)phosphonic acid, [[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid), and [[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]azanediyl]di(propane-3,1-diyl)]bis(phosphonic acid), X-ray diffraction structure determination and analysis at 2.55-2.9 A resolution |
| 2.4.2.8 | free enzyme or enzyme complexed with IMP, hanging drop vapour diffusion method, 20°C, 10 mg/ml protein in 20 Tris-HCl, pH 7.4, mixed with a molar excess of IMP, 0.001 ml protein solution mixed with equal volume of reservoir solution containing 0.2 M magnesium acetate tetrahydrate, 0.1 M sodium cacodylate, pH 6.5, 12% w/v PEG 4000, or protein solution with 1 mM IMP mixed with reservoir solution containing 15% PEG 8000, 0.1 M sodium cacodylate, pH 6.5, 0.2 M magnesium acetate tetrahydrate, X-ray diffraction structure determination and analysis at 2.2-2.5 A resolution |
| 2.4.2.8 | in complex with T-705-RMP, hanging drop vapor diffusion method, using 0.2 M NaCl, 1 M sodium/potassium tartrate, 0.1 M imidazole, pH 8.0 |
| 2.4.2.8 | mutant enzyme D150A, crystallization complexed with xanthosine 5'-monophosphate, diphosphate and 2 Mg2+, post transition state structure analysis, active site structure |
| 2.4.2.8 | purified enzyme in complex with inhibitor [3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid and ([3-(guanine-9-yl)-2-((2-phosphonoethoxy)-methyl)propoxy]methyl)phosphonic acid, hanging drop method, mixing of 0.001 ml of 11.1 mg/ml protein in 0.1 M Tris-HCl, 0.01 M MgCl2, 1 mM DTT, and 0.3 mM 5-phospho-alpha-D-ribose 1-diphosphate, pH 7.4, and 4.8 mM inhibitor, with 0.001 ml of reservoir solution containing 20% PEG 3350, 0.2 M sodium bromide, 0.1 M Bis-Tris propane, pH 7.5, at 18°C, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement and modeling |
