EC Number   |
|---|
    3.5.1.54 | purified enzyme free or in complex with the substrate analog malonate, hanging-drop vapor diffusion method, mixing of 4 mg/ml protein in 10 mM HEPES, pH 8.0, 50 mM NaCl, and 1 mM DTT, with reservoir solution in a 1:1 ratio to a final volume of 0.005 ml, the latter containing 100 mM PIPES, pH 6.5, and 1.04 M sodium malonate, room temperature, 2 months, followed by microseeding, 5-15 days, X-ray diffraction structure determination and analysis at 2.2-2.8 A resolution, molecular replacement |
| 3.5.1.54 | purified full-length wild-type enzyme and truncated mutant enzyme, trypsin-treated AtzF (in situ proteolysis) from 1 M ammonium sulfate, 1 M lithium sulfate, 0.1 M Tris-HCl, pH 8.5, AtzF467 crystals grown from 20% w/v PEG 6000, 0.1 M Na MES pH 6.5, 0.2 M calcium chloride, are used in microseeding for truncated AtzF crystal growth from 11% w/v PEG 3350, 2% Tacsimate, pH 5.0, X-ray diffraction structure determination and analysis at 2.5 A resolution |
| 3.5.1.54 | purified recombinant amidase domain of allophanate hydrolase, AtzF467, X-ray diffraction structure determinations and analysis at 2.5 A resolution |
| 3.5.1.54 | purified recombinant His-tagged enzyme, sitting drop vapor diffusion method, mixing of protein in 0.5 mM urea, 0.5 mM ADP, and 0.5 mM sodium malonate, pH 7.0, with reservoir solution containing 0.1 M Tris/HCl, pH 7.5, 0.2 M ammonium sulfate, 12% PEG 8000, and 2% PEG 3350, X-ray diffraction structure determination and analysis at 6.5 A resolution, modelling by molecular replacement method using the structures of KlUC (PDB 3VA7) and KlAH (PDB 4ISS) as search models |
| 3.5.1.54 | purified recombinant wild-type and mutant enzymes, from a reservoir containing 11 to 14% w/v PEG 3350 and 2% Tacsimate reagent, pH 5.0, at 20°C, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement |
| 3.5.1.54 | purified recombinant wild-type and mutant His-tagged SeMet-substituted enzymes, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 20 mM Tris/HCl, pH 7.5, 200 mM NaCl, 2-10 mM DTT, with reservoir containing 16% PEG 8000, 20% glycerol, and 0.04 M potassium phosphate, and 100 mM sodium/potassium tartrate, 20°C, X-ray diffraction structure determination and analysis at 2.5-2.6 A resolution, molecular replacement |
| 3.5.1.54 | three-dimensional structure analysis using PDB ID 4GYS |
