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. 2023 Feb 16;14:890. doi: 10.1038/s41467-023-36441-z

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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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Fig. 4 — CryoEM map A and model B of C5b9-CD59 complexes comprised of 2 molecules of C9 (C9₁ and C9₂). (C) A model for the C5b9-CD59 complex comprised of 3 C9 molecules. Complement proteins are colored (C5b, grey; C6, blue; C7, orange; C8α pink, C8β magenta, C8γ light purple); CD59 is cyan. The membrane, not visible in the sharpened map, is schematized for reference. D, E Density for the C5b9₂-CD59 map after density subtraction and focused refinement (transparent surface) overlayed with the model. D For the terminal C9 (C9₂, yellow), only the first transmembrane β-hairpin has unfurled while TMH2 (red) remains helical. E CD59 (cyan) deflects both TMH1 and TMH2 from the first C9 (C9₁, green) to block membrane insertion. F The C9₁-CD59 interaction interface. The key residues that mediate interactions are shown as sticks. G Electrostatic surface representation of CD59 highlighting positively charged residues (R55, R53, K38) that interact with the C9 glycan extending from N394 (green sticks). Coulombic potential calculated for the CD59 model in B ranging from −10 (red) to +10 (blue) kcal/(mol·e).