EC Number |
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3.2.1.20 | - |
3.2.1.20 | 10 mg/ml purified protein with 5 mM inhibitor D-(+)-glucono-1,5-lactone, hanging drop vapour diffusion method, 1 ml reservoir solution containing 20% v/v 2-propanol, 20% w/v PEG 4000, 0.1 M sodium citrate, pH 5.6, plus 0.01 ml of a solution consisting of 0.004 ml reservoir solution, 0.005 ml protein solution, containing 1% protein w/v in 10 mM phosphate, pH 7.0, and 0.001 ml inhibitor 50 mM, 2-3 weeks, X-ray diffraction structure determination at 2.5 A resolution |
3.2.1.20 | apoenzyme and enzyme complexed with acarbose, X-ray diffraction structure determination and anaylsis at 2.0 A and 1.9 A resolution, respectively |
3.2.1.20 | crystal structure of the enzyme is determined to a 2.0 A resolution, by X-ray crystallography |
3.2.1.20 | purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, 2-5 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 20 mM NaCl, 0.002 ml protein solution is mixed with 0.003 ml reservoir solution and equilibrated against 1 ml reservoir solution, different compositions of the reservoir solution result in different crystal forms, overview, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5-4.2 A resolution |
3.2.1.20 | purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, hexameric crystal form, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5 A resolution, structure modelling of domains, full-length enzyme, and active site |