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Related Experiment Videos

Visualizing filamentous actin on lipid bilayers by atomic force microscopy in solution.

D Shi1, A V Somlyo, A P Somlyo

  • 1Department of Molecular Physiology & Biological Physics, University of Virginia School of Medicine, Box 800736, Charlottesville, VA 22908-0736, U.S.A.

Journal of Microscopy
|March 10, 2001
PubMed
Summary
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Atomic force microscopy (AFM) visualized actin filament (F-actin) surface structure in aqueous solution. This high-resolution imaging revealed F-actin

Area of Science:

  • Biophysics
  • Cell Biology
  • Structural Biology

Background:

  • Actin filaments (F-actin) are essential cytoskeletal components.
  • High-resolution imaging of F-actin surface structure is crucial for understanding its function.
  • Previous methods faced limitations in resolving fine structural details in aqueous environments.

Purpose of the Study:

  • To visualize the surface structure of actin filaments (F-actin) at high resolution using atomic force microscopy (AFM).
  • To determine key structural parameters of F-actin, including its diameter and helical pitch.
  • To assess the utility of AFM for studying F-actin and associated proteins.

Main Methods:

  • Utilized atomic force microscopy (AFM) in contact mode in aqueous solution.
  • Prepared large F-actin paracrystals on positively charged lipid monolayers for enhanced stability.

Related Experiment Videos

  • Analyzed high-resolution AFM images to resolve surface features and measure dimensions.

    • Main Results:

    • Successfully visualized the right-handed helical surface structure of F-actin at high resolution.
    • Resolved the long pitch (38 nm) and monomer repeat (5.8 nm) of F-actin directly.
    • Determined an F-actin diameter of 10 +/- 1 nm, consistent with X-ray diffraction data.
    • Observed an inter-filament distance of 8 +/- 1 nm, suggesting filament interdigitation.

    Conclusions:

    • AFM provides high-resolution surface structure visualization of F-actin in aqueous solution.
    • The method allows for direct resolution of F-actin's helical pitch and monomer dimensions.
    • This technique offers a stable and accessible approach for studying F-actin and its interactions with other proteins.