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. 2023 Sep 14;8(10):1834–1845. doi: 10.1038/s41564-023-01469-w

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© The Author(s) 2023

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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Extended Data Fig. 6 — The single particle map of the S. lophii ribosome shows no densities for hibernation factors found in the microsporidian species V. necatrix and P. locustae. a, b Atomic model of the V. necatrix ribosome (multicolour) fitted into the density map of S. lophii (transparent grey; L1 stalk density shown as green surface and tRNA density shown as beige surface). The hibernation factor MDF1 blocking the mRNA and tRNA binding sites (green ribbon) is shown in a and the hibernation factor MDF2 occupying the polypeptide exit tunnel (PET) is shown with the same colour in b. c, d Close-up views of hibernation factors MDF1 and MDF2 from the V. necatrix structure. e, f Atomic model of the P. locustae ribosome (multicolour) fitted into the density map of S. lophii (transparent grey; L1 stalk density shown as green surface and tRNA density shown as beige surface). The hibernation factor Lso2 is shown as a green ribbon, occupying the tRNA P- site in e. g, h Close-up views of hibernation factor Lso2 from the P. locustae structure.