EC Number   |
|---|
   1.9.6.1 | homology modeling of structure, the substrate channel and catalytic pocket are more basic than other NapA proteins, which may influence the substrate binding as well as product release |
| 1.9.6.1 | purified recombinant NapDNHis/NapA complex, small angle X-ray scattering analysis, modelling |
| 1.9.6.1 | sitting-drop vapour-diffusion method, crystals of the oxidized form of this enzyme are obtained using polyethylene glycol 3350 as precipitant. A single crystal diffracted to beyond 1.5 A at the ESRF (ID14-1), which is the highest resolution reported to date for a nitrate reductase. The unit-cell parameters are a = 142.2, b = 82.4, c = 96.8 A, beta = 100.7°, space group C2, and one heterodimer is present per asymmetric unit |
| 1.9.6.1 | vapor diffusion method |
| 1.9.6.1 | X-ray diffraction structure analysis, resolution 2.2 A, PDB ID 2jio, modelling |
