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. 2020 Jul 28;10:12618. doi: 10.1038/s41598-020-69313-3

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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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Localization and flexibility of the L31 ribosomal protein. Ribosomal proteins (black) and rRNA (grey) are shown in cartoon. L31, involved in cross-linking, is highlighted in orange. (A) Annotation discrepancy of L31 in the crystal structure (4V4H) in comparison to an recent cryo-EM structure (5U9F). The orange arrow indicates the annotated localization at the ribosomal structure. (B) Two distinct conformations of the CTD of L31. In orange, the first conformation is shown, where cross-links #66, #71–72 and #74 are satisfied. In green, the second conformation is shown, where cross-links #27–30 and #39 are satisfied and cross-link #38 (orange line) is only minorly violated (38.8 Å). Cross-link #26, located in the NTD, is satisfied in both conformations. The images of protein structures were generated with PyMOL (Version 2.3.2), Schrödinger, LCC. https://pymol.org.