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. 2020 Oct 29;11:5466. doi: 10.1038/s41467-020-19278-8

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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. 5 — a A ribbon representation of the dimeric MORC4 ATPaseCW structure. The CW domain is colored yellow, and the ATPase domain is colored green in protomer A and gray in protomer B. The positively charged clusters in ATPaseCW are indicated by ovals and labeled. The residue E56, required for the catalytic activity of ATPaseCW, is also shown in red. b–f EMSA with 601 DNA in the presence of increasing amounts of indicated mutants of MORC4 ATPaseCW.