title: Helical reconstruction of frozen-hydrated scallop myosin filaments.
abstract: Native myosin filaments from scallop striated muscle that have been rapidly frozen in relaxing solutions appear to be well preserved in vitreous ice. Electron micrographs of samples at -177 degrees C were recorded with an electron dose of 10 e/A2 at 1.5 microns defocus. After filament images were straightened by spline-fitting, several transforms showed well-defined layer-lines arising from the helical structure of the filament. A set of 17 near-meridional layer-lines has been collected and corrected for background and for phase and amplitude contrast functions. Preliminary helical reconstructions from this still incomplete data set reveal aspects of structure that were not apparent from earlier analysis of negatively stained filaments from scallop muscle. Individual pear-shaped myosin heads now appear to be well resolved from each other and from the filament backbone. The two heads of each myosin molecule appear to be splayed apart axially. The reconstructions also reveal that the filament backbone has a polygonal shape in cross-section, and that it appears to contain seven peripherally located subfilaments.
authors.affiliation: Rosenstiel Basic Medical Sciences Research Center, Brandies University, Waltham, MA 02254-9110.
authors.forename: P
authors.initials: P
authors.lastname: Vibert
mesh_terms: D000818:Animals; D005583:Fourier Analysis; D005615:Freezing; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron; D008974:Mollusca; D009218:Myosins / Q000737:chemistry / Q000648:ultrastructure*; D015203:Reproducibility of Results
chemical_list: D009218:Myosins