EC Number |
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3.5.1.105 | crystal structure is determined at resolutions of 1.54 A |
3.5.1.105 | crystal structure is determined at resolutions of 2.0 A |
3.5.1.105 | hanging drop vapor-diffusion method, the crystal structure of the enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose demonstrates that Arg92, Asp115, and His152 side chains interact with hydroxyl groups of the glucose moiety of the non-reducing-end GlcNAc residue |
3.5.1.105 | purified enzyme in complex with 2-deoxy-2-methylphosphoramido-D-glucose, hanging drop vapor diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 10 mM MPG, 20 mM Tris-HCl, pH 8.1, and 150 mM NaCl, with 0.001 ml of reservoir solution containing either 0.4 M ammonium phosphate (reservoir 1) or 100 mM sodium acetate, pH 4.6, 10 mM CoCl2, and 1 M 1,6-hexanediol (reservoir 2), equilibration against 0.4 ml of reservoir solution, 20°C, X-ray diffraction structure determiantion and analysis at 1.8-1.9 A resolution, modelling |
3.5.1.105 | purified recombinant enzyme, hanging drop vapor diffusion method, mixing of 20 mg/ml protein in 20 mM sodium phosphate, pH 7.0, with an equal volume of reservoir solution containing 0.1 M Tris-HCl, pH 7.0, 10% w/v PEG 8000, and 0.2 M MgCl2, 4 weeks, 20°C, X-ray diffraction structure determination and analysis at 1.35 A resolution |
3.5.1.105 | the native enzyme and its selenomethionine derivative are crystallized and analyzed in the presence and absence of cadmium ion |