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N. Crampton, M. Yokokawa, D. Dryden, J. Edwardson, D. Rao, K. Takeyasu, et al., “Fast-Scan Atomic Force Microscopy Reveals That the Type III Restriction Enzyme EcoP15I is Capable of DNA Translocation and Looping,” Proceedings of the National Academy of Sciences of the United States of America, Vol. 104, No. 31, 2007, pp. 12755-12760. http://dx.doi.org/10.1073/pnas.0700483104

has been cited by the following article:

• TITLE: AFM Investigation of the Organization of Actin Bundles Formed by Actin-Binding Proteins

  AUTHORS: Jamie L. Gilmore, Masahiro Kumeta, Kunio Takeyasu

  KEYWORDS: F-Actin; Caprice; α-Actinin

  JOURNAL NAME: Journal of Surface Engineered Materials and Advanced Technology, Vol.3 No.4A, October 22, 2013

  ABSTRACT: AFM is a powerful technique for revealing the morphological features of various biological systems at high resolution. However, one of the complications of AFM is that samples must be attached to a flat surface in order to obtain images. This often requires the development of specialized methods depending on the sample which is being used. In this study, we developed a novel technique to image actin bundles on the mica surface. Using this technique, we were able to image molecular assemblies of F-actin with two actin remodeling proteins: α-actinin and Caprice. High resolution AFM images of F-actin fibers and bundle organization depicted two different types of molecular assemblies: F-actin bundles forming an elongated “zipper” structure in the presence of α-actinin, and bundles forming a perpendicularly crossing the mesh structure in the presence of Caprice.