EC Number   |
|---|
    2.4.1.25 | - |
| 2.4.1.25 | crystallized in 2 forms, I and II, form I crystals belongs to hexagonal space group P6(4)22, form II crystals to orthorhombic space group P2(1)2(1)2 |
| 2.4.1.25 | crystals belong to space group P6(4) with cell parameters a = b = 154 A and c = 64 A |
| 2.4.1.25 | Gtase, hanging drop method, inhibitor complex,crystals belong to space group I222, unit-cell dimensions a = 92.6 A, b = 180.3 A, c = 199.2 A, free Gtase crystals a = 94.5 A, b = 181.4 A, c = 197.3 A |
| 2.4.1.25 | hanging drop vapor diffusion method at 25°C, crystal structure of the enzyme with and without an inhibitor, acarbose. The acarbose-bound structure clarifies that Glu123 and Asp214 are the catalytic nucleophile and acid/base catalyst, respectively |
| 2.4.1.25 | hanging drop vapor diffusion method, using 2.0 M ammonium sulfate and 0.1 M bis-tris methane (pH 6.5) |
| 2.4.1.25 | hanging drop vapor diffusion method, using 20% (w/v) PEG-3350 |
| 2.4.1.25 | hanging-drop vapor-diffusion method |
| 2.4.1.25 | hanging-drop vapour-diffusion method. Crystal diffracts to 2.0 A resolution and belongs to space group C222(1), with unit-cell parameters a = 69.7, b = 120.3, c = 174.2 A |
| 2.4.1.25 | purified recombinant enzyme, hanging drop vapour diffusion method, 0.003 ml of protein solution containing 10 mM MES-NaOH, pH 6.5, with 1 mM dithiothreitol is mixed with 0.001-0.003 ml of reservoir solution containing 0.4-0.8 M sodium malonate, pH 5.6, and 1 mM dithiothreitol, equilibration against reservoir solution at room temperature, 1 week, for enzyme-acarbose complexing the crystals are soaked in 0.5 ml of 0.8 M sodium malonate, pH 5.6, with 5 mg/ml acarbose and with or without and 4-deoxyglucose, for 30 min, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution |
