EC Number   |
|---|
   3.1.1.86 | crystal structure refined to a resolution of 1.12 A using synchrotron data collected at 263 K |
| 3.1.1.86 | crystallized in two crystal forms, an orthorhombic and a trigonal crystal form. In the orthorhombic crystal form, the covalently bound carbohydrate at one of the two N-glycosylation sites is involved in crystal contacts. The orthorhombic crystal form is obtained at pH 5.0 and the trigonal crystal form at pH 4.5 |
| 3.1.1.86 | crystals used for structure determination are grown in 1.4 M Li2SO4, 0.1 M Na acetate pH 5.0 with a protein concentration of 40 OD280. The crystals belong to the space group P212121 with a = 52.14 A, b = 56.87 A and c = 71.89 A and one molecule in the asymmetric unit.The structure of RGAE is determined at 1.55 A resolution. RGAE folds into an alpha/beta/alpha structure. The active site of RGAE is an open cleft containing a serine-histidine-aspartic acid catalytic triad. The position of the three residues relative to the central parallel beta sheet and the lack of the nucleophilic elbow motif found in structures possessing the alpha/beta hydrolase fold shows that RGAE does not belong to the alpha/beta hydrolase family |
| 3.1.1.86 | hanging-drop vapour-diffusion method |
| 3.1.1.86 | vapour-diffusion method, the crystal structure of rhamnogalacturonan acetylesterase D192N is determined to 1.33 A resolution and refined to an R value of 11.6% for all data. The structure is virtually identical to the high-resolution (1.12 A) structure of the wild-type enzyme except for the interactions involving the mutation and a disordered loop |
