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. 2019 Feb 20;2:72. doi: 10.1038/s42003-019-0311-z

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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. 6 — Particle polymorphism and self-assembly mechanisms of shrimp nodavirus. a Cryo-EM image of the PvNV-LP. The diameters of the PvNV-LPs are near 35 and 24 nm, corresponding to the T = 3 and T = 1 particles. T = 3 and T = 1 capsids are indicated by white solid and dotted arrows, respectively. Scale bar = 100 nm. b The elution profiles of the PvNV-LP and pET21-PvNV-LP in the size-exclusion chromatography. The various fractions were collected and their absorbance at 280 nm were measured. c Cryo-EM, X-ray crystal and EM structures of the T = 3 and T = 1 PvNV-LPs, T = 1 ΔN-ARM-PvNV SVP and T = 1 ΔN-ARM-PvNVSd SVP. The T = 3 PvNV-LP surface and two T = 1 SVPs surfaces are rainbow-colored according to their distance from the spike to shell. d The diagram shows the putative self-assembly process of the T = 3 and T = 1 shrimp nodavirus capsids. The basic unit of capsid assembly is the dimeric capsomeres (diamond with black solid and dotted lines). The N-ARM deletion and the N-terminal fusion tag both might guide the assembly of the T = 1 capsid