Extended Data Fig. 4: Cryo-EM data processing.

A. Data processing workflow for the REGN5381 Fab + NPR1 ectodomain + ANP complex, including particle orientation distribution and FSC curve for the final reconstruction. B. Final map coloured by local resolution, from 2.5 to 5.5 Å. C. A sample of the EM density at the NPR1:REGN5381 interface, with selected residues labelled. D. A cutaway view of the EM density, sliced through the centre of the dimer to reveal the density at the peptide binding site. Density surface is coloured by molecule: REGN5381 Fab heavy chain – salmon; light chain – grey; NPR1 monomers – green and cyan (mostly hidden); ANP – purple; unassigned density – white. E. Data processing workflow for the REGN5381 Fab + NPR1 ectodomain (no ANP) complex. F. 3D FSC isosurface at FSC = 0.143, oriented with the lowest resolution along the z axis and the best resolution along the x axis, and coloured radially by resolution as indicated in the colour key. G. Local resolution map, oriented to show the absence of the ANP peptide in this complex. H. A sample of the EM density for this complex. I. A cutaway view of the EM density, sliced through the centre of the dimer to reveal the lack of density at the peptide binding site. Density surface is coloured by molecule: REGN5381 Fab heavy chain – salmon; light chain – grey; NPR1 monomers – green and cyan (mostly hidden); unassigned density – white. ANP, atrial natriuretic peptide; EM, electron microscopy; FSC, Fourier shell correlation; NPR1, natriuretic peptide receptor.