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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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Visualization of differences in X-ray and cryo-EM structures, identified by cross-links falling in the mixed-type category, and localization of the trigger factor. Ribosomal proteins (black) and rRNA (grey) are shown in cartoon. (A) Capturing the flexibility between the 30S and 50S subunits. In the X-ray structure (4V4H), cross-links #62 and #73 are satisfied (yellow dashed lines); in the cryo-EM-structure (5U9F), a different conformation is visible, which violates the maximum distance (red dashed lines). (B) Structural model of the trigger factor (orange) in complex with the E. coli ribosome. Cross-link satisfaction is indicated as yellow lines, violation as orange lines. The known low-resolution structure (2VRH) is superimposed and shown in magenta. The images of protein structures were generated with PyMOL (Version 2.3.2), Schrödinger, LCC. https://pymol.org.