EC Number   |
|---|
   3.2.1.78 | - |
| 3.2.1.78 | both native protein and selenomethionyl derivative, enzyme expressed in Pichia pastoris |
| 3.2.1.78 | crystallization of catalytic domain. Crystals from conditions with phosphate or citrate salts as precipitant belong to space group P212121, resolution to 1.4 A, while a crystal from a condition with ethanol as precipitant belongs to space group I212121, resolution to 1.45 A |
| 3.2.1.78 | enzyme in apoform and in complex with mannopentaose, the precipitant solution contains 25% w/v PEG 3350, 0.1 M Tris-HCl, pH 8.5, X-ray diffraction structure determination and analysis, modelling |
| 3.2.1.78 | hanging drop vapor diffusion |
| 3.2.1.78 | hanging drop vapor diffusion method, using 1 M ammonium citrate, 15% (v/v) isopropanol, and 0.1M Tris-HCl (pH 8.5) |
| 3.2.1.78 | hanging drop vapour diffusion method, mixing of 6.5 mg/ml protein in 20 mM Tris-HCl, pH 7.6, with reservoir solution containing 0.1 M magnesium chloride, 0.1 M sodium acetate pH 4.5, 23% w/v PEG 3350, 20°C, method optimization, X-ray diffraction structure determination and analysis at 1.40 A resolution, molecular replacement |
| 3.2.1.78 | hanging-drop vapor diffusion method at room temperature |
| 3.2.1.78 | homology modeling of structure |
| 3.2.1.78 | molecular dynamic simulation of wild-type and mutant lacking the C-terminal amino acid residues 394-399, SerLysLeuSer. The inactive form has a lower stability than the active one. The loss of amino acids from the C-terminal end of the protein indirectly affects the conformation of the catalytic Glu318 residue and stability of active site because of interactions between residues at the C-terminus and the rest of protein |
