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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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Primary and modelled structures of SAVSBPM18-Linker-Dextran-binding domain (M18-L-DBD), and its purification and immobilization to Sephadex. (a) Organization of various domains [engineered streptavidin SAVSBPM18, linker, dextran-binding domain (DBD) and a short C-terminal tail sequence (T)] in M18-L-DBD. Amino acid residues that mark the boundary of the domains are listed. (b) A modelled structure of M18-L-DBD. The four subunits in SAVSBPM18 are colored in red, yellow, green and blue, respectively. DBD is colored in purple. (c) SDS-PAGE showing intracellular production of M18-L-DBD in E. coli BL21[pET29B-M18-L-DBD]. (d) Purification of M18-L-DBD using biotin-agarose. Fractions were analyzed by SDS-PAGE. (e) SDS-PAGE analysis of the binding of M18-L-DBD to Sephadex G-100. All samples in panels c–e were boiled before loading. Arrowhead indicates the position of M18-L-DBD. M, molecular weight markers (sizes in kDa); S, intracellular soluble fraction; I, intracellular insoluble fraction; FT, flow-through fraction; W, wash fractions; E, elution fractions; BF, bound fraction. Gel profiles shown in panels c, d and e are from different gels.