EC Number   |
|---|
    4.1.3.3 | - |
| 4.1.3.3 | complexed with sialic acid alditol, 4-deoxy-sialic acid or 4-oxo-sialic acid, microbatch crystallization, hanging drop vapor diffusion method |
| 4.1.3.3 | L142R mutant, complexed with beta-hydroxypyruvate, hanging drop vapor diffusion method |
| 4.1.3.3 | ligand-free and (2R)-sialic acid alditol-bound enzyme, hanging drop vapor diffusion method, using |
| 4.1.3.3 | mutant enzyme E192N, in complex with pyruvate, sitting drop vapor diffusion method, using 100 mM Tris-HCl pH 8.2, 200 mM ammonium acetate, 18% PEG 3350 |
| 4.1.3.3 | purified recombinant enzyme, hanging drop vapour diffusion method, 0.002-0.0025 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, is mixed with 0.0017-0.0022 ml of reservoir solution containing 25% w/v PEG 3350, 200 mM ammonium sulfate, 100 mM Bis-Tris pH 5.5, equilibration against 1 ml of reservoir solution, 8-20°C, method optimization, X-ray diffraction structure determination and analysis at 1.7 A resolution, molecular replacement |
| 4.1.3.3 | purified recombinant His-tagged wild-type enzyme, wild-type enzyme with Schiff base and in complex with pyruvate, mutant K164A enzyme, and mutant K164A in complex with N-acetylneuraminic acid and N-glycolylneuraminic acid, hanging drop vapour diffusion method, crystals of wild-type PmNAL from 21% PEG 1000, 150 mM NaCl, and 100 mM Na2HPO4/KH2PO4, pH 6.2. PmNAL K164A mutant in ligand-free from from 30% PEG 200, 100 mM NaCl, and acetate, pH 4.5. Crystals of the PmNAL K164A mutant bound to ligands are grown in 38% PEG 300, 0.01 M CaCl2, and 0.1 M sodium cacodylate, pH 6.5. The sialic acid concentration was 5 mM, X-ray diffraction structure determination and analysis at 1.75-2.10 A resolution, molecular replacement modeling |
| 4.1.3.3 | purified recombinant wild-type enzyme and mutants K165C variant and K165-gamma-thialysine, alone or in complex with pyruvate, hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution containing 8 mg/ml protein in 50 mM, pH 7.4, with 0.002 ml of reservoir solution containing 100 mM Tris-HCl, pH 7.0-8.5, 200 mM NaCl, and 18-28% w/v PEG 3350, pyruvate complexes of the wild-type and K165-gamma-thialysine mutant enzymes crystals are soaked in the mother liquor containing 100 mM sodium pyruvate and 15% v/v PEG 400 for 1 min before being sequentially transferred to mother liquor with 5% increments in PEG 400 concentration. The final soak contains the mother liquor containing 100 mM sodium pyruvate and 25% v/v PEG 400, 18°C, X-ray diffraction structure determination and analysis at about 2.0 A resolution, molecular replacement |
| 4.1.3.3 | recombinant enzyme in complex with N-acetylneuraminate and acetyl-D-mannosamine/pyruvate, soaking in the mother liquor containing 15% w/v PEG400, then 20% w/v PEG400, and subsequently for 5 min in 25% w/v PEG400 containing 75 mM Neu5Ac, X-ray diffraction structure determination and analysis |
| 4.1.3.3 | sitting drop diffusion method, PEG 3350 |
