title: Structural studies of synthetic filaments prepared from column-purified myosin.
abstract: Synthetic filaments prepared from column-purified rabbit skeletal myosin by slow dialysis exhibit characteristic bipolar organization and 14-nm axial subunit spacing. Backbone substructure can be discerned in high resolution micrographs in the form of striations of 3--4-nm width and slight angular tilt from the direction of the filament axis. Filament backbone diameters vary over the population, although remaining relatively constant for a single filament. Approximately 25% of the filaments appear poorly stained and frayed, which may be due to collapse on the electron microscope grid. Optical diffraction studies reveal a 43-nm axial repeat as well as the 14.3-nm subunit repeat, indicating a structural homology with natural filaments. A model for synthetic filament aggregation is presented that is consistent with observations of backbone diameter variation, absence of bare zones, and the presence of fraying filaments.
mesh_terms: D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003599:Cytoskeleton / Q000648:ultrastructure*; D008854:Microscopy, Electron; D008968:Molecular Conformation; D009218:Myosins / Q000302:isolation & purification; D011817:Rabbits
chemical_list: D009218:Myosins
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