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. 2022 Nov 28;613(7945):775–782. doi: 10.1038/s41586-022-05573-5

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 8 — a. Low pass filtered (10 Å) cryo-EM reconstructions of both major (transparent grey) and minor (solid, colored) configurations are aligned with respect to TnsB. The dashed box indicates the TnsC-DNA interactions at the TnsB proximal region shown as inset in panel B. b. Three TnsB-proximal TnsC protomers (From TnsC1 to TnsC3) in both major and minor configurations interact with target strand DNA (tsDNA) in an identical manner through residue R182. Hydrogen bonding interactions (distance cut off <4 Å) between protein residues and the sugar-phosphate backbone of DNA are represented with dashed lines. Base pairs that are interacting with TnsC are represented as filled nucleotides and stick phosphate-backbone.