Organization of mitochondrial ATP synthase dimers and their membrane-bending properties. (A) Tomographic slice through an intact mitochondrion of Podospora anserina; yellow arrowheads mark the location of the ATP synthase dimers. (B) Three-dimensional reconstruction of the data in A; yellow spheres indicate the catalytic domains in the ATP synthase dimers against the cristae membrane (cyan). (C) Curvature perturbation caused by an isolated ATP synthase dimer along the direction parallel to the dimer long axis, from CG molecular dynamics simulations. (D) Same as C, along the direction perpendicular to the dimer. (E) Same as D, for a row of four ATP synthase dimers, arranged side by side as observed in mitochondrial cristae. Note that the membrane is flat between adjacent dimers along the direction of the row. In the perpendicular direction, the membrane profile is nearly identical to that in C. A and B are adapted from Davies et al. (2011), and C and D are adapted from Davies et al. (2012).