Abstract
The subunit organization of the myosin filament of chicken striated muscle has been observed directly in cross-sections in electron microscopy. The organization consists of three centrally located and nine peripherally located subunits in a close-packed arrangement. This arrangement is that predicted by a previously derived model for the detailed molecular organization of the myosin filament (Pepe, 1966 a, 1967 a, 1971). Each subunit measures approximately 30 A in diameter and the center-to-center distance is approximately 37 A. If these measurements are considered to be on the high side, then they indicate that each subunit represents one myosin molecule. However, it is not possible to determine unequivocally whether one or two myosin molecules per subunit are present on the basis of this work.