Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. I. Tilt angle of myosin subfragment-1 in the rigor complex.
A three-dimensional image of the "rigor" complex of actin and chymotryptic myosin subfragment-1 was reconstituted from electron micrographs of negatively stained specimens. Data went out to 20 A radially and 26 A axially. The reconstituted images allowed us to deduce the angle between the major axis of the main part of myosin subfragment-1 and the axis of the actin helix. The subfragment-1 molecules were attached to the actin filament in a configuration in which they were tilted by only about 15 degrees from the plane perpendicular to the axis of the actin helix. The implication of the smaller tilt angle than the commonly accepted value is discussed.
D000199:Actins; D000818:Animals; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008958:Models, Molecular; D009132:Muscles / Q000648:ultrastructure*; D009218:Myosins; D011487:Protein Conformation; D011817:Rabbits
D000199:Actins; D046911:Macromolecular Substances; D009218:Myosins