EC Number   |
|---|
    1.17.1.9 | by adding polyethylene glycol No. 6000 |
| 1.17.1.9 | hanging drop vapor diffusion method |
| 1.17.1.9 | hanging drop vapor diffusion method, using 2.3 M ammonium sulfate in 0.1 M bis Tris buffer pH 6.5 (for the holoenzyme bound to NAD+ and azide) or 2.2 M ammonium sulfate and 2% (w/v) PEG 400 in 0.1 M HEPES buffer pH 7.5 (for the apoenzyme) |
| 1.17.1.9 | in complex with formate, molecular replacement method. Four protein molecules per asymmetric unit, forming two dimers identical to the dimer of apoenzyme. The sulfur atom of C354 exists in the oxidized state |
| 1.17.1.9 | in complex with NAD+ and azide |
| 1.17.1.9 | in complex with NADH. The biologically active dimer is formed by the crystallograohic rotation axis. Comparison with structure of apoenzyme and enzyme-NAD+-azide triple complex |
| 1.17.1.9 | re-evaluation of crystallographic data |
| 1.17.1.9 | sitting drop vapor diffusion method, using 0.1 M HEPES pH 7.0, 25% (w/v) polyethylene glycol 6000, 1.2 M lithium chloride |
| 1.17.1.9 | sitting drop vapour diffusion method with 0.1 M sodium-cacodylate pH 6.5, 0.15 M ammonium sulfate, 30% (w/v) PEG 8K (mutant K47E), and 0.1 M sodium cacodylate pH 6.0, 0.2 M ammonium sulfate, and 32.5% (w/v) PEG 8K (mutant K328V) |
