A comprehensive structural model of F1FO ATP synthase from E. Coli reveals a rotational mechanism which allows the enzyme to change conformation in order to perform its crucial task of generating cellular energy through the conversion of proton motive force to ATP. Citation: "Visualizing movements in E. coli F1FO ATP synthase indicates how the F1 and FO motors are coupled" Meghna Sobti, James L. Walshe, Robert Ishmukhametov and Alastair G. Stewart. (2019)