Extended Data Fig. 4: Exemplary electron density maps of NosD.
From: Molecular interplay of an assembly machinery for nitrous oxide reductase

a, The maps section shows a stereo representation of the electron density map around the HMM motif of NosD as indicated in the cartoon of the complex. In the ATP-bound state of the NosF(E154Q) variant complex, the HMM motif (residues H297, M209, M231) are metal-free. b, Electron density map for the NosDFYL complex in GDN micelles, showing the same region as in (a). Zn2+ binds to NosL and Cu+ is coordinated by the HMM motif of NosD. c, As the NosZDFY complex was formed with the NosF(E154Q) variant that produces a NosDFY complex that cannot receive Cu from NosL, the metal sites of the apo enzyme are vacant. Electron density map at the CuA site of N2OR. The structure of the holo form of the enzyme (right) underlines the absence of the two Cu ions. d, Electron density map at the CuZ site in the hub of the β-propeller domain of N2OR. The Cu-replete protein in the same orientation (right) denotes where the tetranuclear cluster should be located. All maps are normalized and contoured at the 5σ level.