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. 2022 Jul 7;5:675. doi: 10.1038/s42003-022-03640-1

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© The Author(s) 2022

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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Fig. 1 — a Each gene, ftsA, minD and minE, was placed under its own T7 promoter, ribosome binding site and T7 transcription terminator and was constitutively expressed with PUREfrex2.0 in test-tube reactions. b Quantitative LC-MS analysis of FtsA, MinD and MinE protein production after 3 h of expression at 37 °C. Abundance of the most C-terminal proteolytic peptide was quantified for each protein using an internal standard (QconCAT). Data represent mean values over three biological repeats, each analyzed in three technical replicates. c Concentration of FtsA, MinD and MinE (most C-terminal peptide) as a function of the expression time course (from 0 to 6 h). Symbols represent data from three independent experiments. The solid lines are fits to a mathematical model for gene expression kinetics (Methods section).