Figure 7. Monomeric mitochondrial F₁F_o ATP synthase as the factor determining cristae membrane curvature.

(A) Schematic diagram of bovine F₁F_o ATP synthase in the 2D crystal lattice, with its transmembrane F_o stator domain imposing a local 43° kink and a 16° inclination of the c-ring relative to the crystal plane. Blue, stator; red, rotor. (B) Schematic diagram of a single monomeric bovine F₁F_o ATP synthase. CS: central stalk; PS: peripheral stalk; IMS: intermembrane space; TM F_o: transmembrane domain of F_o. (C) Association of two monomeric F₁F_o complexes into a dimer results in an angle of 86°, as observed in ATP synthase dimers in mitochondrial cristae (Davies et al., 2012).

DOI: http://dx.doi.org/10.7554/eLife.06119.020