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. 2019 Jun 26;10:2806. doi: 10.1038/s41467-019-10577-3

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© The Author(s) 2019

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 — AcrIIC2_Nme functions as a homodimer. a The crystal structure of AcrIIC2_Nme solved by Se-SAD reveals a dimeric protein containing both α-helical and β-strand structural elements. Monomers are colored in violet and deep salmon, and the N- and C-termini are noted. b Cartoon representation of AcrIIC2-Nme1Cas9 complex. c Surface representation of AcrIIC2-Nme1Cas9 complex. d Electrostatic surface potential of AcrIIC2-Nme1Cas9 complex. e, f Interactions between the bridge helix and AcrIIC2_Nme. The bridge helix is shown in cyan. AcrIIC2.1 and AcrIIC2.2 are shown in violet and deep salmon, respectively