EC Number   |
Reference |
|---|
    3.5.1.2 | - |
209011, 209022, 209023, 209032, 696266 |
| 3.5.1.2 | by addition of ammonium sulfate |
663903 |
| 3.5.1.2 | C-terminally truncated enzyme, hanging-drop, vapor-diffusion method at 25°C, X-ray diffraction structure determination and analysis at 2.4 resolution using multiple-wavelength anomalous dispersion, MAD |
667444 |
| 3.5.1.2 | catalytic domain of isoform KGA in complex with 6-diazo-5-oxo-L-norleucine, hanging drop vapor diffusion method, using 0.1 M Bis-Tris propane (pH 7.2) and 1.8 M LiSO4 |
735259 |
| 3.5.1.2 | determination of the structures of the intact enzyme in the presence and in the absence of its product L-glutamate and its activator Tris, which activates the enzyme by 6fold, and in the presence of both |
711989 |
| 3.5.1.2 | enzyme and its fragment containing about 80% of the protein, handing-drop vapour-diffusion method |
654091 |
| 3.5.1.2 | handing-drop vapor diffusion technique, at 18ºC |
656222 |
| 3.5.1.2 | molecular modeling of structure and docking with the substrate and potential inhibitors |
755388 |
| 3.5.1.2 | phosphate- and L-glutamate-bound GAC, X-ray diffraction structure determination and analysis at 2.85 A and 2.80 A resolution, respectively |
720930 |
| 3.5.1.2 | purified recombinant GAC free and in complex with inhibitor bis-2-(5-phenylacetimido-1,2,4,thiadiazol-2-yl)ethyl sulfide, hanging drop vapor diffusion, mixing of protein in 25 mM HEPES (pH 7.5), 200 mM NaCl, 5% glycerol, and 5 mM beta-ME, with reservoir solution containing 0.3 M magnesium chloride, 0.1 M Tris, pH 8.5, and 12% w/v PEG 4000, X-ray diffraction structure determination and analysis at 2.55 and 2.3 A resolution, respectively |
718889 |
