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. 2023 Dec 20;625(7993):195–203. doi: 10.1038/s41586-023-06870-3

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a, Cryo-EM map and model of PP2A:B55–tpARPP19. Two views of the map (top) with the corresponding view of the molecular model (bottom). b, Cryo-EM map and model of PP2A:B55–FAM122A. c, Overlay of PP2Aa from the PP2A:B55 crystal structure (PDB ID: 3DW8; beige) and the PP2A:B55–inhibitor model (grey), superimposed using HEAT repeats 1–6. d, Rotated view of the experimental map. e, Overlay of the PP2Ac catalytic domains from PP2A:B55-FAM122A (cyan) and PP2A:B56 (brown; PDB ID: 2IAE); the C-terminal tails (amino acids R294–mL309) shown as surfaces. f, B55 shown as surface and coloured by sequence conservation; ARPP19 (orange) and FAM122A (slate blue) are shown as ribbons.