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. 2021 Sep 9;12:5329. doi: 10.1038/s41467-021-25682-5

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — A Workflow of capped filament preparation for cryo-EM. Monomers were mixed with CP followed by Ca^2 +-to-Mg^2 +exchange and salt addition to trigger polymerization. Polymerization was arrested by phalloidin addition and capped filaments were separated from free CP by size-exclusion chromatography (SEC) and then visualized by cryo-EM. B Isolation of short, capped actin-filaments from free CP by SEC from a representative run. The experiment was repeated at least 5 times with similar results. Top: chromatography profile. Bottom: Corresponding Coomassie-stain with bands representing actin or α and β-capping protein as indicated (Supplementary Fig. 1). C Representative micrograph of vitrified capped filaments on graphene oxide grids imaged at 1.5 µm defocus. Similar results were obtained in at least five independent replicates. The inset shows the corresponding power spectrum for the image. Bottom: Class averages showing densities for capping protein bound to respective filament barbed ends.