Muscle contraction consists of a cyclical interaction between myosin a
nd actin driven by the concomitant hydrolysis of adenosine triphosphat
e (ATP). A model for the rigor complex of F actin and the myosin head
was obtained by combining the molecular structures of the individual p
roteins with the low-resolution electron density maps of the complex d
erived by cryo-electron microscopy and image analysis. The spatial rel
ation between the ATP binding pocket on myosin and the major contact a
rea on actin suggests a working hypothesis for the crossbridge cycle t
hat is consistent with previous independent structural and biochemical
studies.