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. 2019 Mar 4;9:3359. doi: 10.1038/s41598-019-40044-4

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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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Binding of the fluorescently labelled monomeric His-SC-L-DBD(Cys) and tetrameric M18-L-ST·His-SC-L-DBD(Cys) to Sephadex G-100 beads. (a,b) Domain organization of His-SC-L-DBD(Cys) and M18-L-ST·His-SC-L-DBD(Cys). HT, His-tag; Cys, cysteine; M18, SAVSBPM18; ST, SnoopTag; SC, SnoopCatcher; DBD, Dextran-binding domain. (c) Spatial and temporal distribution of fluorescently labelled monomeric His-SC-L-DBD(Cys) and tetrameric M18-L-ST·His-SC-L-DBD(Cys) to Sephadex G-100 beads. Labelled protein binding to Sephadex was analyzed up to 120 days after mixing the labelled proteins with the beads. Surface distribution of the fluorescently labelled molecules is the major focus of these pictures.