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. 2018 Sep 10;9:3668. doi: 10.1038/s41467-018-06078-4

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© The Author(s) 2018

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. 1 — Architecture of the HSV-2 C-capsid. a Surface representation of HSV-2 C-capsid. The table lists the major capsid elements as identified by color in the capsid. b Cryo-EM map of an asymmetric unit and local electron density maps are shown. The inset shows the density map (mesh) and atomic model of VP5 which illustrate side chain features. Residues with side chains are labeled, aa denotes amino acids. c Ribbon diagram of the atomic model of an asymmetric unit. The triplex consists of two VP23 conformers (denoted as VP23-1 and VP23-2) and one copy of VP19C. UL36-CT denotes UL36 C-terminal helix. The CVSC comprises a UL17 monomer, two UL25 conformers (denoted as UL25-1 and UL25-2) and two UL36 conformers (denoted as UL36-1 and UL36-2). Rainbow ribbon models show individual proteins and conformers (blue N terminus through green and yellow to red C terminus)