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. 2017 Oct 16;7:13260. doi: 10.1038/s41598-017-13550-6

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© The Author(s) 2017

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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MOSP^Fl contains N- and C-terminal domains with different solubility properties. (A) Domain architecture of MOSP^Fl predicted by InterProScan. The first 20 amino acids (shown in green) contain the cleaved signal sequence. The portion of MOSP^Fl colored in blue denotes the N-terminal domain, MOSP^N, while red denotes the C-terminal domain, MOSP^C. (B) Optimal model for MOSP^Fl, generated by I-TASSER, predicting a bipartite architecture in which MOSP^N, contains substantial α-helical content and MOSP^C is predominantly β-sheet. (C) Overlay of models generated by I-TASSER predicting that MOSP^C is a 10-stranded β-barrel. (D) 10 µg of recombinant MOSP^Fl, MOSP^C, MOSP^N and Skp were phase-partitioned in TX-114 and separated on SDS-PAGE. Lanes show detergent-enriched and aqueous phases probed with antisera directed against each recombinant protein. Panel D presents cropped images; the full-length images are presented in Supplementary Figure 4.