Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. IV. Reconstitution from minimal- and high-dose images of the actin-tropomyosin-myosin subfragment-1 complex.
Three-dimensional images of the actin-tropomyosin-myosin subfragment-1 (S1) complex were reconstituted from both minimal- and high-dose electron micrographs by using a conventional reconstruction technique. Higher resolution (1/15 A-1) than those of the previous reconstructions was attained. A multi-domain structure similar to that of the actin-S1 complex described in the previous paper (1) was observed and a ne diagram of the multi-domain structure of the actin-tropomyosin-S1 complex is presented. The shape of S1 molecules in the rigor complex was clearly resolved. In a view perpendicular to the filament axis, S1 had an axially bent profile; only the tail portion, which was thin but was not small in diameter, was steeply inclined. These features were more prominent in the model from minimal-dose images than that from high-dose images.
D000199:Actins; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003599:Cytoskeleton / Q000648:ultrastructure*; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008958:Models, Molecular; D008961:Models, Structural; D009132:Muscles / Q000648:ultrastructure*; D015879:Myosin Subfragments; D009218:Myosins; D010446:Peptide Fragments; D011487:Protein Conformation; D011817:Rabbits; D014335:Tropomyosin
D000199:Actins; D046911:Macromolecular Substances; D015879:Myosin Subfragments; D010446:Peptide Fragments; D014335:Tropomyosin; D009218:Myosins