PMC

Representative electron micrograph of rotor rings in vitreous buffer (scale bar, 10 nm).Gold‐standard FSC curve for the density map of the rotor ring in LDAO. The resolution at 0.143 FSC was 6.1 Å (arrow).

A–DRepresentative 2D class averages of the rotor ring showing the ring from the side and top as well as slices through 3D maps after refinement for (A) LDAO, (B) DDM, (C) C₁₂E₈, and (D) amphipol A8‐35.ETop view of the rotor ring in LDAO with 17 identical hairpin‐like c‐subunits fitted.FSide view of the c‐ring in LDAO with the refined model fitted. The helices in the outer ring are slightly shorter than the inner helices. Two adjacent c‐subunits form a functional ion‐binding unit. The positions of residues involved in ion binding or defining the membrane boundary are shown in different colors.

SDS–PAGE of the isolated B. pseudomallei c‐ring before and after TCA treatment, which dissociates the complex into monomers.Western blot of the B. pseudomallei N‐ATPase in Burkholderia membranes with a specific anti‐c‐subunit antibody. The rotor ring shows the same oligomeric size as the isolated complex in (A).Negative‐stain electron microscopy of the B. pseudomallei N‐ATPase β‐subunit with immunogold‐labeled His₆‐tag in inverted membrane vesicles.

Local density of states (LDOS) in the middle of a planar S-N-S junction versus one in the middle of a ring junction of same width. The rotor peak at E/Δ = 0.088 is present only in the ring junction.