This review deals with the structure of the actin monomer, its assembly into filaments and the loci on F-actin involved in binding myosin. Two distinctly different arrangements of monomers have been suggested for actin filaments. One model proposed by Holmes et al. is well developed. It places the so-called 'large' domain close to the filament axis and the so-called 'small' domain out near the surface of the filament. A second, less-well developed, model proposed by Schutt et al. locates the 'small' domain close to the filament axis and they rotate the monomer so that 'bottom' of the 'large' domain is at the highest radius. We analyze the available evidence for the models of F-actin derived from X-ray diffraction, reconstructions from electron micrographs, fluorescence resonance energy transfer spectroscopy, chemical cross-linking, antibody probes, limited proteolysis, site-directed and natural mutations, nuclear magnetic resonance spectroscopy and other techniques. The result is an actin-centered view of the loci on actin which are probably involved in its interaction with the myosin 'head'. From these multiple contacts we speculate on the sequence of steps between the initial weak-binding state of S-1 to the actin filament through to the stable strong-binding state seen in the absence of free Mg-ATP, i.e., the rigor state.