EC Number   |
|---|
   3.5.1.26 | - |
| 3.5.1.26 | D151N mutant AGA precursor, complexed with glycine and without glycine |
| 3.5.1.26 | hanging drop vapor diffusion technique, 1.9 A resolution, precursor and autoprocessed enzymes |
| 3.5.1.26 | mutant with lower turnover number to be able to get a crystal with natural substrate in complex |
| 3.5.1.26 | purified recombinant enzyme mutant T203I free and in complex with N4-(beta-N-acetylglucosaminyl)-L-asparagine, hanging drop vapor diffusion technique, mixing of 2mg/ml protein solution with reservoir oslution containing 0.2 M NaCl, 0.1 M bis-Tris, pH 6.5, and 25% PEG 3350, cryoprotection in solution containing 100 mM Tris-HCl, pH 8.0, and 20% glycerol, X-ray diffraction structure determination and analysis, molecular replacement using the structure of the wild-type enzyme (PDB ID 2GAW) as the starting model |
| 3.5.1.26 | purified recombinant enzyme mutant T99K free and in complex with substrate N4-(beta-N-acetylglucosaminyl)-L-asparagine, hanging drop vapor diffusion technique, mixing of 2mg/ml protein solution with reservoir oslution containing 0.2 M NaCl, 0.1 M bis-Tris, pH 6.5, and 25% PEG 3350, cryoprotection in solution containing 100 mM Tris-HCl, pH 8.0, and 20% glycerol, X-ray diffraction structure determination and analysis at 1.5 A resolution, molecular replacement using the structure of the wild-type enzyme (PDB ID 2GAW) as the starting model |
| 3.5.1.26 | purified recombinant mutant G172D enzyme precursor in presence of L-aspartic acid beta-hydroxamate, X-ray diffraction structure determination and analysis at 2.1 A resolution. Structures of the precursor and the mature form are found in a single crystal |
