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. 1979 Sep;27(3):423–432. doi: 10.1016/S0006-3495(79)85226-1

Structural studies of synthetic filaments prepared from column-purified myosin.

J F Koretz
PMCID: PMC1328597  PMID: 263630

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.

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425FIGURE 1
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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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