ArticleBiophysical journal2000
Cryoatomic force microscopy of filamentous actin.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Semiflexible Biopolymers in Bundled Arrangements.Polymers · 2016Review
- Nanostructured self-assembly of inverted formin 2 (INF2) and F-actin-INF2 complexes revealed by atomic force microscopy.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- Review
- 3D nanometer images of biological fibers by directed motion of gold nanoparticles.Nano letters · 2011Article
- Atomic force microscopy reveals drebrin induced remodeling of f-actin with subnanometer resolution.Nano letters · 2011Article
- The human IgM pentamer is a mushroom-shaped molecule with a flexural bias.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Application of calorimetry, sub-ambient atomic force microscopy and dynamic mechanical analysis to the study of frozen aqueous trehalose solutions.Pharmaceutical research · 2008Article
- An historical perspective on cell mechanics.Pflugers Archiv : European journal of physiology · 2008Article
- The role of high-resolution imaging in the evaluation of nanosystems for bioactive encapsulation and targeted nanotherapy.Micron (Oxford, England : 1993) · 2007Review
- The high-resolution architecture and structural dynamics of Bacillus spores.Biophysical journal · 2005Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Cryoatomic force microscopy (cryo-AFM) was used to image phalloidin-stabilized actin filaments adsorbed to mica. The single filaments are clearly shown to be right-handed helical structures with a periodicity of approximately 38 nm. Even at a moderate concentration ( approximately 10 microg/ml), narrow, branched rafts of actin filaments and larger aggregates have been observed. The resolution achieved is sufficient to resolve actin monomers within the filaments. A closer examination of the images shows that the branched rafts are composed of up to three individual filaments with a highly regular lateral registration with a fixed axial shift of approximately 13 nm. The implications of these higher-order structures are discussed in terms of x-ray fiber diffraction and rheology of actin gels. The cryo-AFM images also indicate that the recently proposed model of left-handed F-actin is likely to be an artifact of preparation and/or low-resolution AFM imaging.
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Registered trials
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