View from above and then below the F1 domain along the rotating γ-subunit. (8.2 Mb)
The rotary mechanism of mitochondrial ATP synthase. (12 Mb)
Changes in the positions of sidechains in the catalytic site of F1-ATPase bringing about binding and subsequent hydrolysis of ATP. (8.9 Mb)
How the rotating γ-subunit imposes the conformational states on a β-subunit required for substrate binding, ATP formation and ATP release. (4.5 Mb)
Three conformations of a catalytic β-subunit produced by 120º rotations of the central γ-subunit. (2.5 Mb)
