EC Number   |
|---|
    1.1.1.6 | - |
| 1.1.1.6 | crystal obtained by hanging-drop vaour-diffusion method, S305C mutant |
| 1.1.1.6 | crystallization as a contaminant, crystal was initially assumed to be of a mutant of the SurE protein as it shares some structural features with the presumed target protein |
| 1.1.1.6 | hanging drop vapour diffusion, mixing of 0.001 ml 6 mg/ml protein in 150 mM ammonium acetate, 50 mM sodium chloride, 20 mM Tris, pH 7.4, 5% glycerol with 0.001 ml reservoir solution containing 5-10% PEG 3350, 0.2 M calcium acetate, and 4% glycerol, X-ray diffraction structure determination and analysis at 1.90 A resolution, molecular replacement using PDB entry 1jpu as a search model |
| 1.1.1.6 | in presence of glycerol |
| 1.1.1.6 | preliminary X-ray characterization |
| 1.1.1.6 | sitting drop vapor-diffusion method |
| 1.1.1.6 | sitting-drop vapor-diffusion method at 22°C, solved at 2.8 A resolution. Each GldA monomer consists of nine beta-strands, thirteen alpha-helices, two 3(10)-helices and several loops organized into two domains, the N- and C-terminal domains. The active site is located in a deep cleft between the two domains |
| 1.1.1.6 | structure containing glycerol in the active site, to 2.8 A resolution. Each GldA monomer consists of nine beta-strands, thirteen alpha-helices, two 310-helices and several loops organized into the N- and C-terminal domains. The active site is located in a deep cleft between the two domains. The N-terminal domain contains a classic Rossmann fold for NAD+ binding. The glycerol molecule is sandwiched by the Zn2+ and NAD+ ions |
| 1.1.1.6 | structure of mutant D121N/F245S |
