Skip to main content
. Author manuscript; available in PMC: 2018 May 18.
Published in final edited form as: Science. 2018 Apr 5;360(6384):eaao7298. doi: 10.1126/science.aao7298

Fig. 1. Cryo-EM reconstruction and atomic modeling of the HSV-1 capsid.

Fig. 1

(A) Radially colored cryo-EM density map of the HSV-1 capsid viewed along a threefold axis. Fivefold, threefold, and twofold axes are denoted by a pentagon, triangle, and oval, respectively. (B) Magnified view of one facet of the icosahedral capsid with structural components differentially colored. The density of triplex Tf at the center is not shown. (C) A schematic representation of one asymmetric unit (shaded) of the capsid. An extra copy of triplex Te (unshaded) from an adjacent asymmetric unit is shown to depict that triplex pair Tb-Te has a similar configuration as Ta-Tc, thus providing a second potential binding site for the CATC (11, 17). The enlarged red and blue triangle shows the heterotrimeric nature of a triplex. a.a., amino acid. (D) Atomic models of individual capsid or tegument proteins in rainbow-colored ribbon (from blue at the N terminus to red at the C terminus). Numbers denote chain termini or flexible segments that are not modeled. a.a., amino acid.