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. 2019 Jan 23;9:364. doi: 10.1038/s41598-018-36247-w

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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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Ectoine synthase-catalyzed enzyme reaction scheme, purification and quaternary assembly of the (Pl)EctC protein. (a) Scheme of the ectoine synthase catalyzed cyclo-condensation of the substrate N-γ-ADABA to form ectoine. (b) Coomassie brilliant blue stained 15% SDS-polyacrylamide gel with different amounts of the affinity chromatography purified (Pl)EctC-Strep-tag II protein. The PageRuler Prestained Protein Ladder (Thermo Scientific) was used as a sizing marker. A picture of the original SDS-gel can be found in Fig. S1. (c) SEC-MALS analysis to determine the quaternary assembly of the purified (Pl)EctC-Strep-tag II protein.