3.5.4.5 - 209642, 209665, 209668 3.5.4.5 comparison of theoretically predicited model and experimentally elucidated structure 669910 3.5.4.5 crystal structure of tetrameric cytidine deaminase at 2.0 A resolution, hanging drop vapour-diffusion method 654638 3.5.4.5 hanging drop vapor diffusion method 712889 3.5.4.5 hanging drop vapour diffusion method. R56A and R56Q crystallize in the same space group as the wild-type enzyme with two subunits in the asymmetric unit, whereas C53H/R56Q can not crystallize in this crystal form but is crystallized in another space group, P3(2)21, with a full tetramer in the asymmetric unit 654757 3.5.4.5 in complex with inhibitor diazepinone riboside. Inhibitor is able to establish a canonical pi/pi interaction with key active site residue F137 669792 3.5.4.5 in complex with tetrahydrouridine, 3-deazauridine, or cytidine. Two alternate conformations of R68 influence zinc-product interaction 667736 3.5.4.5 purified CDA in complex with uridine and deoxyuridine, hanging drop vapor diffusion method, 0.002 ml of 12 mg/ml protein in 20 mM Tris-HCl pH 7.5 is mixed with 0.002 ml of reservoir solution containing 0.1 M HEPES, pH 7.5 and 4.3 M sodium chloride, ligands uridine and deoxyuridine are added by soaking method, X-ray diffractiuon structure determination and analysis at 2.4 and 1.9 A resolution,molecular dynamics simulation, structure modeling 718695 3.5.4.5 purified recombinant CDA complexed with either tetrahydrouridine, 3-deazauridine, or cytidine, hanging drop vapor diffusion technique, 25°C, protein solution, containing 10-15 mg/ml protein in 20 mM Tris-HCl, pH 7.5, 1 mM DTT, and 5 mM ligand, is mixed with crystallization solution containing 2.0 M ammonium sulfate and 0.1 M Tris-HCl, pH 8.5, crystals appear after a few hours or several days, respectively, X-ray diffraction structure determination and analysis at 1.48-2.36 A resolutions, molecular replacement 667736 3.5.4.5 structures of apomutants E47D and E47Q 755377 3.5.4.5 to 2.07 A resolution. Two 1,4-dioxane moleules are present at the active site 752690