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. 2021 Sep 29;12:5706. doi: 10.1038/s41467-021-25948-y

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© The Author(s) 2021

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 — In vitro aminoacylation of qtRNAs using EcSerRS (a), EcArgRS (b), and EcTyrRS (c); qtRNA^Trp_UAGA was used as a negative control in all cases. d Analysis of EcGlnRS identity elements as found in the engineered qtRNA^Trp_UAGA and qtRNA-PACE evolved qtRNA^Trp_UAGA-Evo1. e Anticodon and adjacent nucleobase identities for known E. coli glutamine tRNAs and the qtRNA-PACE evolved qtRNA^Trp_UAGA-Evo1. Position of the modified nucleotide cmnm⁵s²U (yellow) in the co-crystal structure of tRNA^Gln_CAA and E. coli GlnRS (4JYZ; https://www.wwpdb.org/pdb?id=pdb_00004jyz). Data represent the mean and standard deviation of three biological replicates.