EC Number |
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2.4.1.4 | cocrystallization of E328Q mutant enzyme with maltoheptaose, X-ray structure at 2.2 A resolution |
2.4.1.4 | crystal structure of the acid/base catalyst mutant, E328Q, with a covalently bound glucopyranosyl moiety. The structure is refined to a resolution of 2.2 A and shows that binding of the covalent intermediate results in a backbone movement of 1 A around the location of the nucleophile, Asp286 |
2.4.1.4 | crystal structure of wild-type amylosucrase in complex with beta-D-glucose at 1.66 A, crystal structure of E328Q mutant enzyme in complex with sucrose at 2.0 A resolution |
2.4.1.4 | purified recombinant detagged DgAS, free and in complex with turanose, hanging drop vapor diffusion method, X-ray diffraction structure determination and analysis at 1.97-2.10 A resolution |
2.4.1.4 | purified recombinant detagged NpAS in complex with turanose, hanging drop vapor diffusion method, 1:1 v/v ratio of protein, containing 6 mg/ml in 20 mM Tris, pH 8.0, to precipitant solution containing 1.5 M sodium acetate, 0.1 M sodium cacodylate, pH 7.0, 2 weeks, X-ray diffraction structure determination and analysis at 1.85 A resolution |
2.4.1.4 | purified wild-type and mutant ligand-free enzyme, hanging drop vapour diffusion method, mixing of 0.0025 ml of 3.3 mg/ml protein in 50 mM HEPES, pH 7.0, 150 mM NaCl, 1 mM EDTA, and 1 mM DTT, with 0.0025 ml of reservoir solution containing 1 M sodium acetate, 0.1 M imidazole, 0.1 M LiCl, pH 6.5, 4°C, X-ray diffraction structure determination and analysis at 3.15 A resolution, modeling |
2.4.1.4 | recombinant enzyme, equal amounts of 4 mg/ml enzyme in 150 mM NaCl, 50 mM Tris-HCl, pH 7.0, 1 mM EDTA and 1 mM dithiothreitol and reservoir solution consisting of 30% polyethylene glycol 6000 and 100 mM HEPES, pH 7.0, crystal structure at 1.4 A resolution |
2.4.1.4 | the mutant enzyme R226K/I228V/A289I/F290Y/E300I/V331T/Q437S/N439D/C445A is crystallized by hanging drop vapor diffusion method at 12°C |