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. 2021 Feb 3;590(7847):671–676. doi: 10.1038/s41586-021-03197-9

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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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Extended Data Fig. 3 — a, Cryo-EM map representing TS1, coloured by local resolution in Å as estimated by ResMap. The map was generated using our TS1 ABP for the complex representing UBE2L3~ubiquitin~ARIH1 bound to neddylated CUL1–RBX1–SKP1–SKP2–CKSHS1–p27–cyclin A–CDK2. b, Fourier shell correlation curve (FSC) displaying an overall resolution of 3.83 Å with the FSC = 0.143 criterion. c, Structure shown in electron microscopy density. Left, close-up of E3–E3act domain, showing side-chain density for interactions between the RING domain of RBX1 and the Ariadne domain of ARIH1. Middle, close-up of E3–E3 platform showing interactions with UBE2L3-linked ubiquitin. Right, ubiquitin transferase module. The map quality permitted modelling of side chains either visible in the density or by wholesale docking of previous crystal structures. d, Cryo-EM map representing TS2, coloured by local resolution in Å as estimated by ResMap. The map was generated using our TS2 p27 ABP for the complex representing ARIH1~ubiquitin~p27 bound to CUL1–RBX1–SKP1–SKP2-CKSHS1. This particular map is from a complex using ARIH1(F430A/E431A/E503A), which was previously shown to relieve autoinhibition and bypass the need for neddylation⁴. e, FSC curve displaying an overall resolution of 3.91 Å with the FSC = 0.143 criterion. f, Structure shown in electron microscopy density, representing highest, medium and lowest resolution areas of the map. Left, close-up of E3–E3act domain, showing side-chain density for interactions between the RING domain of RBX1 and the Ariadne domain of ARIH1. Middle, portion of CUL1. Right, ubiquitin transferase module. After the ubiquitin transferase module was modelled and refined for the structure representing TS1, it was wholesale-docked into the lower-resolution density for this region in the cryo-EM maps representing TS2.