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. 2022 Feb 8;12:2061. doi: 10.1038/s41598-022-06073-2

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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The phage CBA120 TSP quaternary complex. (A) The c(s) distribution profiles of 3.3 μM each of TSP1, TSP2, TSP3 and TSP4-N₃₃₅. (B) Summary of the protein–protein interactions revealed by the AUC experiments. TSP domains are colored as in Fig. 1. Primary domain-domain interactions that presumably utilize the same threefold symmetry axes are indicated by solid blue arrows. Protein–protein interactions that presumably do not occur through shared threefold symmetry axes are indicated by dashed blue arrows. (C) Molecular model of the quaternary TSP complex. Left: Stereoscopic representation of the space filling model showing TSP1 (blue), TSP2 (magenta), TSP3 (orange) and TSP4 (green). Right: Ribbon representation using the same color scheme.