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. 2020 Feb 13;53:6. doi: 10.1186/s40659-020-00274-7

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 4 — Optimal conditions for Cu⁺ ATPase activity mediated by CtpB. The Cu⁺ ATPase activity was measured using plasma membranes isolated from M. smegmatis mc²155 expressing CtpB and membranes isolated from M. smegmatis transformed with the expression vector pMV261. The enzymatic parameters evaluated were: a temperature, b pH, and c cysteine concentration. The data correspond to the mean ATPases activity ± SEM derived from measurements of technical triplicate