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. 2019 Apr 16;9:6169. doi: 10.1038/s41598-019-42229-3

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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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TEM images of protein aggregation and trimer-dimer formation. Panel (a) uranyl acetate negative staining of protein for JO-4 (left), GB3_V239D (middle), and GB7_V239D (right). The white arrows indicate aggregates which appear nearly 50 nM in diameter according to the 50 nM size bar in white at the lower left of the figure. Panel (b) the space-filling model of the trimer-dimer of JO-4 was created in VMD 23 using the known x-ray crystallographic coordinates of JO-4. The model depicts a barbell shape with an approximate length of 11.5 nm and a width of 7 nm. Panel (c) fine resolution enhancement images of white specks seen in the GB7_V239D image in panel a. The images reveal structures resembling the barbell structure in both size and shape of the modeled trimer-dimer.