EC Number   |
|---|
    3.5.1.4 | crystallized using the hanging-drop vapour-diffusion method. Crystals produced in the presence of 1.2 M sodium citrate, 400 mM NaCl, 100 mM sodium acetate pH 5.6 are selected for X-ray diffraction studies. A data set having acceptable statistics to 1.96 A resolution is collected under cryoconditions using an in-house X-ray source. The space group is determined to be primitive cubic P4(2)32, with unit-cell parameter a = 130.49 A |
| 3.5.1.4 | hanging-drop technique at both 16 and 4°C, rhombohedral morphology |
| 3.5.1.4 | high resolution crystallographic structure shows that each amidase monomer is formed by a globular four-layer alphabetbetaalpha sandwich domain with an additional 81-residue long C-terminal segment. This wraps arm-in-arm with a homologous C-terminal chain of another monomer, producing a strongly packed dimer. In the crystal, the biological active homo-hexameric amidase is built grouping three such dimers around a crystallographic 3fold axis |
| 3.5.1.4 | native enzyme using the hanging-drop vapour-diffudion technique, a His-tagged protein cannot be crystallized |
| 3.5.1.4 | purified recombinant His-tagged enzyme, hanging drop vapour diffusion, from 0.1 M sodium acetate trihydrate, and 2 M ammonium sulfate, pH 4.6, single wavelengh X-ray diffraction structure determination and analysis at 1.7 A resolution |
| 3.5.1.4 | purified recombinant wild-type RhAmidase and mutant S195A in complex with benzamide, hanging drop vapor diffusion method, 20°C, mixing of 0.002 ml of protein solution containing 14 mg/ml protein in 10 mM Tris-HCl, pH 8.0, with 0.002 ml of reservoir solution containing 15% w/v PEG 4000, 100 mM magnesium chloride, 100 mM calcium chloride, 100 mM MES, pH 6.0, X-ray diffraction structure determination and analysis at 2.17 A and 2.32 A resolution, respectively, molecular replacement method |
| 3.5.1.4 | purified wild-type enzyme, 25 mg/ml protein in 50 mM Tris-HCl, pH 7.2, containing 5 mM DTT and 1 mM EDTA, hexagonal crystals, X-ray diffraction structure determination and analysis at 1.25-1.4 A resolution |
| 3.5.1.4 | purified wild-type enzyme, 25 mg/ml protein in 50 mM Tris-HCl, pH 7.2, containing 5 mM DTT and 1 mM EDTA, hexagonal crystals, X-ray diffraction structure determination and analysis at 1.25-1.4 A resolution, modeling |
| 3.5.1.4 | the crystal structure of amidase at a resolution of 1.9 A is solved by molecular replacement from a crystal belonging to the primitive cubic space group P4232 |
