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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. 7 — a, OsCas12f. Yhe apo protein exits as a monomer, and gRNA binding triggers dimer formation. Docking of RuvC.2 domain is required for full R-loop formation. b, Al3Cas12f. The apo protein exits as a dimer and full R-loop formation occurs before RuvC.2 domain docking. c, RhCas12f. The apo protein exits as a monomer and gRNA binding triggers dimer formation. Both RuvC domains remain highly flexible during R-loop formation.