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. 2017 Sep 28;8:722. doi: 10.1038/s41467-017-00718-x

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© The Author(s) 2017

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 — Different conformational states of 100S ribosomes. Rigid-body fits of two 70S models without the C-terminal domains of HPF^long into the low-resolution maps of the two most extreme conformations, closed state (a, b) and open state (c, d). The difference between the two classes depicts a 55° rotation around the interface. The ‘closed’ conformation closely resembles our 5.6 Å map. Colors indicate 16S rRNA (orange), protein uS2 (cyan and purple) and other proteins (blue). The rotation causes H26 to change its interaction from H26 to protein uS2 from the other ribosome, effectively widening the space between the two 70S ribosomes within the dimer (arrows in b, d)