title: Subfilament organization in myosin filaments of the fast abdominal muscles of the lobster, Homarus americanus.
abstract: The myosin filaments of the fast abdominal muscle of the lobster are about 2.7 microns long with a diameter of about 20 nm. They have a low density core in transverse sections except for a short portion in the middle of the filaments about 140 nm in length which is solid. In the solid region the diameter of the filaments is 25 nm. The wall of the filaments is made up of 12 subfilaments arranged in six pairs in a single layer around the wall. The spacing between the subfilaments of a pair is 3.4 nm and the spacing between successive pairs is 8.4 nm. An extra density is present on the inner surface of the wall of the filament along the entire length of the tubular portion of the filament. This density is always adherent to the wall and in serial transverse sections of the same filament its position changes from section to section without any apparent pattern to the change. No structural organization could be detected in this extra density.
mesh_terms: D008841:Actin Cytoskeleton / Q000648:ultrastructure*; D000818:Animals; D003599:Cytoskeleton / Q000648:ultrastructure*; D008854:Microscopy, Electron; D009132:Muscles / Q000648:ultrastructure*; D009218:Myosins / Q000032:analysis*; D008121:Nephropidae
chemical_list: D009218:Myosins