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. 2026 Apr 13;33(5):756–767. doi: 10.1038/s41594-026-01788-6

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© The Author(s) 2026

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. 4 — a, Model of OsCas12f dimerization interface. b,c, Zoomed-in overview of specific interactions that mediate the interactions among the REC interface in OsCas12f in α1 (b) and loop (c). d, Model of RhCas12f dimerization interface. e,f, Zoomed-in overview of specific interactions that mediate the interactions among the REC interface in RhCas12f in α1 (e) and loop (f). g, Model of Al3Cas12f dimerization interface. h–k, Zoomed-in overview of specific interactions that mediate the interactions among the REC interface in Al3Cas12f in the tenon (h) and REC.1 α3 (i), α1 (j) and α2 (k). l, GFP assays evaluating the effect of different dimerization domain mutants to disrupt specific interactions. Data represent the mean ± s.d. (n = 3 independent biological replicates). Significance was determined using a one-way ANOVA.

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