Cryoatomic force microscopy of filamentous actin

49Citations
Citations of this article
38Readers
Mendeley users who have this article in their library.

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 ~38 nm. Even at a moderate concentration (~10 μg/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 ~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.

Cite

CITATION STYLE

APA

Shao, Z., Shi, D., & Somlyo, A. V. (2000). Cryoatomic force microscopy of filamentous actin. Biophysical Journal, 78(2), 950–958. https://doi.org/10.1016/S0006-3495(00)76652-5

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free