EC Number   |
|---|
   1.13.11.41 | hanging drop vapour diffusion method, mixing of 5 mg/ml protein in 50 mM Tris, pH 7.3, 100 mM NaCl, and mM 4-hydroxybenzoic acid or 0.1 mM 4-aminobenzamidine, with reservoir solution containing 0.1 M sodium cacodylate pH 5.9-6.8 and 1.1-1.6 M sodium acetate, method optimization, X-ray diffraction structure determination and analysis at 1.88 A resolution. The use of limited chymotrypsinolysis, which apparently results in removal of the first 20 or so N-terminal residues of DAD, is necessary for crystallization of the protein |
| 1.13.11.41 | purified recombinant detagged chymotrypsinolysed enzyme, 5 mg/ml protein in 50 mM Tris, pH 7.5, 100 mM NaCl, 1 mM 2-mercaptoethanol is mixed with a solution containing 10% w/v PEG 1000 and 10% PEG 8000, X-ray diffraction structure determination and analysis at 2.2 A resolution. The use of limited chymotrypsinolysis, which apparently results in removal of the first 20 or so N-terminal residues of DAD, is necessary for crystallization of the protein |
| 1.13.11.41 | purified recombinant His-tagged chymotrypsinolysed enzyme, 5 mg/ml protein in 50 mM Tris, pH 7.5, 100 mM NaCl, 1 mM 2-mercaptoethanol is mixed with a solution containing 10% w/v PEG 1000 and 10% PEG 8000, X-ray diffraction structure determination and analysis at 2.2 A resolution. The use of limited chymotrypsinolysis, which apparently results in removal of the first 20 or so N-terminal residues of DAD, is necessary for crystallization of the protein |
