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. 2024 Aug 14;43(19):4384–4405. doi: 10.1038/s44318-024-00195-1

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© The Author(s) 2024

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/. Creative Commons Public Domain Dedication waiver http://creativecommons.org/publicdomain/zero/1.0/ applies to the data associated with this article, unless otherwise stated in a credit line to the data, but does not extend to the graphical or creative elements of illustrations, charts, or figures. This waiver removes legal barriers to the re-use and mining of research data. According to standard scholarly practice, it is recommended to provide appropriate citation and attribution whenever technically possible.

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(A) Surface representation of cryo-EM reconstruction of JBD30 procapsid. Pentamers of major capsid protein are highlighted in light blue, hexamers in turquoise. Positions of selected icosahedral five-, three-, and twofold symmetry axes are indicated. The inset shows an electron micrograph of a JBD30 procapsid. (B) Cartoon representation of major capsid proteins forming pentamer and hexamer of procapsid. Two major capsid proteins (one from the hexamer and one from the pentamer) are coloured according to domains as in panel (D). (C) Comparison of pentamers and hexamers from procapsid and capsid. Sideview of the major capsid protein pentamer and hexamer shown as molecular surfaces. (D) Comparison of major capsid proteins from procapsid and capsid. The major capsid proteins from the procapsid are coloured according to domains. Superimposed major capsid proteins from the capsid are shown in grey. Major differences occur in the position of the N-terminal arm and in the width of the extended loop and peripheral domain. (E) Comparison of interactions of portal complex with capsid proteins and in JBD30 procapsid and capsid. Left: Central slice through composite map of portal complex and procapsid. Right: Central slice through asymmetric reconstruction of capsid–portal interface. Density occupied by the major capsid proteins is shown in blue, density of minor capsid proteins is in yellow, density of the portal protein is coloured according to domain. Scale bars 5 nm.