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. 2020 Oct 16;11:5241. doi: 10.1038/s41467-020-19072-6

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© The Author(s) 2020

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. 3 — a Recognition of the PAM duplex by the WED and PI domains. b The PI domain recognizes the base of T(−2′) via Ala232, and forms extensive hydrogen bonds with the phosphate backbone of the non-target strand. c Most bases of the PAM duplex form extensive hydrogen bonds with either Cas12i2 or other bases within the PAM duplex via waters (red spheres), forming a water-mediated hydrogen bond network. d Mutation of residues forming hydrogen bonds with the PAM sequence substantially reduces the DNA cleavage. e DNA cleavage by Cas12i2 using a linear plasmid DNA containing a mutant PAM sequence. The mutated nucleotide is shown in red and the wild-type sequence is shown in black. f The mutation of the nucleotide T that is directly upstream the PAM sequence shows no effect on Cas12i2 DNA cleavage activity.