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. 2023 Dec 20;625(7995):578–584. doi: 10.1038/s41586-023-06856-1

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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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Extended Data Fig. 3 — a, Crosslinks found between PfRIPR, PfCyRPA and PfRH5 after incubating the reconstituted PfRCR complex with the crosslinker DSSO. Inter-protein crosslinks are blue and intra-protein crosslinks are grey. Crosslinks that are inconsistent with the PfRCR complex structure (with a Cα-Cα distance greater than 35 Å) are indicated by dashed lines. The regions of PfRIPR, PfCyRPA and PfRH5 built in the PfRCR structure are highlighted by a darker tone. The location of EGF5 in PfRIPR is indicated to highlight the intra-PfRIPR crosslink supporting the proposed location of this domain in the PfRIPR structure. Prepared using xiNET⁵⁰. b, Crosslinks with a Cα-Cα distance less than 35 Å mapped on to the PfRCR complex structure.