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. 2021 Sep 23;28(10):799–810. doi: 10.1038/s41594-021-00656-9

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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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Extended Data Fig. 7 — (a) The atomic model of our OAD array (γ-HC removed) fits well into previously reported cryo-ET maps of axoneme structures from four different organisms [human (Homo. sapiens), mouse (Mus. musculus), zebra fish (Danio. rerio), and sea urchin (Strongylocentrotus. purpuratus)]^12,13,40,74, whose OADs contain homologues of α- and β-heavy chains. (b) The top-view structure of the array networks formed by intra- (blue) and inter-OAD (red, yellow) interactions. (c) Enlarged views of the eight main TTH interaction sites. The regions of OAD₀ and OAD _+ 1 involved in interactions are marked in yellow and purple, respectively.