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. 2017 Jul 11;7:5159. doi: 10.1038/s41598-017-05354-5

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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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Negative stain electron micrographs of MbAhpC. (A) Micrograph of MbAhpC in its reduced form showed ring and rod shape particles, which were likely representing the top (red arrow) and side (green arrow) views of the ring structures, respectively. (B) The recombinant and reduced MbAhpC eluted with majority of the protein fractions at approximately 12 ml on a Superdex 200 HR 10/30 column and showed high purity on a 17% SDS gel (inset). (C) 2D classification of MbAhpC particles in its reduced form. Raw particles were classified in 32 classes employing 2D classification procedure of RELION image processing package. (D) Projection analysis revealed a dodecameric MbAhpC. Particles from the boxed classes in C were further classified into 4 classes to improve the quality of 2D classification. (E) The ring-shaped particles seen in the micrographs of reduced MbAhpC above were absent in the micrograph of the oxidized protein.