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. 2019 May 30;10:2366. doi: 10.1038/s41467-019-10272-3

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© The Author(s) 2019

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. 7 — Structure of the lower collar. a Left: Ribbon diagrams showing the lower collar assembly; middle: ribbon diagrams showing two gp11 monomers of the lower collar assembly. One of the two monomers is colored according to its domains (gp11-α1–3: green, gp11-α4–6: red, β-domain: cyan), while the other gp11 monomer is colored gray; right: a zoom-in showing salt bridges in between two gp11 monomers at the wide mouth region of the funnel-shaped lower collar. The scale bar represents 5 nm. b Surface electrostatic potential of the lower collar and the terminal protein gp3. Negative and positive electrostatic potentials are colored red and blue, respectively. Left: outer surface electrostatic potential of the lower collar; middle and right: inner surface electrostatic potential of the lower collar and outer surface electrostatic potential of the terminal protein gp3. c Left: ribbon diagrams showing gp11 α-domain-based structural superimpositions of the mature virion lower collar (blue) and the genome emptied virion lower collar (green). R.m.s.d.s for different portions of the lower collar were calculated and shown at the left side of the superimposition. The r.m.s.d.s shown in the parentheses were calculated from the structural superimpositions by using the upper or the bottom portion of the β-domain; middle: representative densities of the upper and the bottom portions of the β-domains; right: a zoom-in showing the contraction of the lower collar upon genome release