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. 2024 Oct 29;15:9306. doi: 10.1038/s41467-024-53778-1

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© The Author(s) 2024

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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Fig. 2 — a, b View onto the PAM and adjacent dsDNA bound to types IV-A1 (a) and IV-A3 (b) in two 90°-rotated orientations. c and d Close-up view onto the PAM interface in types IV-A1 (c) and IV-A3 (d). Side chains in proximity to the PAM are shown as sticks. The sharpened experimental cryo-EM map is shown as a translucent surface around the side chains and DNA. e λ-vir assay for type IV-A3 probing PAM-interface amino acid substitutions. Plaque Forming Units (PFU) beyond the Limit Of Detection (LOD, countable single plaques) are plotted (blue bars). n = 3 independent spot plate replicates; mean ± s.d. Residues producing interference defects upon substitution are highlighted in bold in panel (d) and Supplementary Fig. 8b. Source data are provided as a Source Data file.