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. 2022 Jul 2;13:3825. doi: 10.1038/s41467-022-31480-4

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© The Author(s) 2022

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. 1 — A Crystal structure of a hAgo2-guide RNA complex (pdb 4W5N). Green dots indicate labeling positions. The amino acids (F23, H291, T511) were mutated to p-azido-L-phenylalanine (AzF) to enable site-specific labeling. B Immobilization strategy to allow single-molecule FRET measurements using TIRF microscopy. C (i) Labeling positions for intermolecular FRET measurements using DyLight^TM550-labeled hAgo2^PAZ and a guide RNA^14Cy5. (ii) FRET efficiency histogram for the setup shown in (i). D (i) Labeling positions of hAgo2^N/Mid for intramolecular FRET measurements. (ii) FRET efficiency histogram for hAgo2^N/Mid. Both histograms show data of at least three independent measurements. Data were fitted to a single Gaussian equation. Source data provided as a Source Data file.