EC Number |
Reference |
---|
3.1.11.1 | by hanging-drop vapor-diffusion method, unbound ExoI, to 1.7 resolution. ExoI bound to the C terminus of ssDNA-binding protein, at 2.7 A resolution. Two C terminus ssDNA-binding proteins bind to adjacent sites on ExoI |
700988 |
3.1.11.1 | crystallization of recombinant wild-type native and selenomethionine-labeled enzyme, and of recombinant mutant D173A enzyme in complex with metal ions, X-ray diffraction structure determination and analysis at 2.5-3.4 A resolution, modelling |
714695 |
3.1.11.1 | hanging-drop vapour-diffusion method at room temperature, structure of ExoI in complex with a nucleotide product, thymidine 5'-monophosphate |
677328 |
3.1.11.1 | in complex with thymidine 5'-monophosphate, hanging drop vapour diffusion method, using 200 mM NaCl, 100 mM Tris-HCl pH 8.5, and 20% (w/v) PEG 8000 |
677328 |
3.1.11.1 | purified enzyme in complex with four different ssDNA substrates, 5'-Cy5-dT13, 5'-Cy5-dA13, dA16 and dT13, hanging drop vapor diffusion, 0.002 ml of 10 mg/ml enzyme in 20 mM Tris, 1 mM DTT, 10 mM EDTA, pH 8.0, with a 1.2 molar excess of oligonucleotide, is mixed with 0.002 ml of reservoir solution containing 0.9-1.5M ammonium sulfate, 3.756.0% 2-propanol and 25% glycerol, 1 week, X-ray diffraction structure determination and analysis at 2.0-3.7 A resolution |
730495 |
3.1.11.1 | sitting drop vapor diffusion method, using 16% (w/v) PEG 4000, 0.1 M Tris pH 8.5, 0.2 M CaCl2 |
749982 |
3.1.11.1 | solubilization of the inclusion bodies is performed by the high-pressure refolding method and highly purified protein is subjected to crystallization by the sitting-drop vapour-diffusion method at 20°C. A crystal of PhoExo I is obtained in a reservoir solution consisting of 0.1 M Tris-HCl pH 8.9, 27% PEG 6000 and diffracts X-rays to 1.52 A resolution. The crystal of PhoExo I belong to space group H32, with unit-cell parameters a = b = 112.07, c = 202.28 A. The crystal contains two PhoExo I molecules in the asymmetric unit |
726637 |
3.1.11.1 | X-ray structure determination |
653308 |