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. 2020 Jun 19;11:3112. doi: 10.1038/s41467-020-16925-y

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© The Author(s) 2020

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. 3 — a–c The cryoEM helical structure of Fab C10:ZIKV catSP. a The cryoEM map surface (left) and different slice-through views (middle and right panels). The map is colored by the regions containing (1) the inner leaflet of the bilayer lipid membrane (red), (2) the transmembrane regions of the E and M proteins (yellow), (3) the ectodomain of the E and M proteins (green) and (4) variable (cyan) and constant regions (blue) of the Fab C10. It also correspond to cylindrical radius: red (30-50 Å), yellow (51-100 Å), green (101–125 Å), cyan (126-150 Å), blue (151-175 Å). b Two turns of the fitted helical structure in two different views. The E proteins, M proteins and the variable region of the Fabs are colored in green, yellow, and purple, respectively. c The superposition of three adjacent asymmetric units consisting in total three E protein dimers of the catSP helical structure (red) with an E protein raft (blue) from the icosahedral spherical mature particle indicating the three asymmetric unit is nearly structurally identical to the raft structure (RMSD is 0.8 Å). d, e The helical cryoEM structure of Fab C10:DENV3 clubSP. d The surface (left) and different slice-through views (middle and right panels) of a segment of the tail of Fab C10:DENV3 clubSP cryoEM map. The map is also colored according to their regions containing different parts of the surface proteins and Fabs similar to (a), but their cylindrical radius are as follows: red (5–10 Å), yellow (11–30 Å), green (31–60 Å), cyan (61–90 Å), blue (91–120 Å). e Approximately two turns of the fitted homology model of Fab C10:DENV3-CH53489 clubSP helical structure in different views, colored as in (b). f Inter-dimer contacts between E protein dimers of catSP (left) and clubSP (right) are very different. There are far fewer E protein inter-dimer contacts in the Fab C10:DENV3 clubSP than the Fab C10:ZIKV catSP. The contacts are colored in red and were identified by using a cutoff distance of 8.0 Å between Cα residues.