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. 2017 Nov 9;7:15227. doi: 10.1038/s41598-017-15151-9

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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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ATPase activity of MsbA reconstituted in PNDs. The ATPase activity of purified MsbA T561C was measured at 37 °C. Values are presented as means ± SEM relative to the activity in detergent (0.35 ± 0.02 s⁻¹). The activity of MsbA in PNDs (n = 12) was significantly higher (~7×) than that of MsbA in detergent (n = 10; P < 0.001).