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. 2020 Jul 30;11:3797. doi: 10.1038/s41467-020-17568-9

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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 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. 4 — a EPR3 binds R7A EPS with a K_d of 38.1 ± 7.5 μM (n = 7). b EPR3 does not bind chitin (CO6) (n = 3). c EPR3 binds R7A de-O-acetylated EPS (deOAc-EPS) with a K_d of 31.3 ± 11.7 μM (n = 3). d EPR3 binds R. leguminosarum (R. leg.) EPS with a K_d of 9.0 ± 3.7 μM (n = 3) and e S. meliloti EPS with a K_d of 221.9 ± 102.3 μM (n = 3). f Overview of the equilibrium-dissociation constants value (K_d) in the 95% confidence interval for the different ligands. The corresponding goodness of fit (R²) are indicated, and (n) represents the number of replicates performed using independent protein preparations. NB no detectable binding.