Extended Data Fig. 8: Subtomogram averaging of prohibitin complexes.

(a) Initial average of the prohibitin complex obtained through subtomogram averaging in Dynamo (3.87 Å pixel size). Left: X-view of the Cryo-EM map displaying a convex structure with a hollow core. Right: Z-view showing a ring-like structure. (b) Fourier shell correlation. A resolution of 28.1 Å (0.143 criterion) was obtained for the average presented in (a). (c) Average after initial alignment of subvolumes with 5 Å pixel size. The cryo-EM map suggests an underlying C11 symmetry of the prohibitin complex. (d) Subtomogram average of volumes with 5 Å pixel size aligned with C11 symmetry. Left: X-view of the average. Right: Top-view of the average. (e) Fourier shell correlation. A resolution of 18.3 Å (0.143 criterion) was obtained for the average presented in (d). (f) Subtomogram average of volumes with 2.5 Å pixel size aligned with C11 symmetry. Left: X-view of the average. Right: Top-view of the average. (g) Fourier shell correlation. A resolution of 16.3 Å (0.143 criterion) was obtained for the average presented in (f). (h) Isosurface representations. The final cryo-EM map with C11 symmetry (green, left), alignment without symmetry (red, middle), and an overlay of both maps (right). Scale bars, 10 nm.