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. 2021 Sep 9;12:500. doi: 10.1186/s13287-021-02565-6

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© The Author(s) 2021

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — Strategies for increasing the donor availability at Cas9 cut site. a Thiol-maleimide chemistry-based Cas9 and ssODN conjugation. A short oligonucleotide adaptor is attached to the Cas9 via thiol-maleimide and appended with ssODN by base pairing. b Cas9-ssODN linking using snap-tag technology. Snap-tag fused Cas9 is covalently linked to the BG coupled ssODN. c RNP-ssODN tethering using HUH endonuclease. Cas9 is fused to the HUH endonuclease PCV Rep protein via H4-2 linker. Then, ssODN is covalently attached to the HUH endonuclease PCV. d In S1mplex system, sgRNA modified using streptavidin-binding aptamer is linked to the biotinylated ssODN, forming RNP-ssODN complex. e Cas9 is fused to the avidin via flexible linker and Cas9 is linked to biotin modified ssODN. f Direct fusion of CtIP and Cas9 nuclease