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. 2020 Sep 23;10:15493. doi: 10.1038/s41598-020-72418-4

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© The Author(s) 2020

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 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/.

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Thermal melting curves of the ancestral and extant IPMDHs. The change in ellipticity at 222 nm was monitored as a function of temperature. The scan rate was 1.0 °C/min. The samples comprised 5.0 μM protein in 20 mM potassium phosphate (pH 7.6), 0.5 mM EDTA. Each experiment was conducted in duplicate with identical melting profiles within experimental error. The plots were normalized with respect to the baseline of the native and denatured states. Green, ancIPMDH-IQ; orange, ancIPMDH-ML; magenta, T. thermophilus PMDH; blue, B. subtilis IPMDH; cyan, S. cerevisiae IPMDH.