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. 2020 Apr 14;11:1814. doi: 10.1038/s41467-020-15610-4

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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 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. 2 — a, b Isomorphous difference density map (F_obs(18fs) – F_{obs(single pulse)})²⁹ of thaumatin at a contour level of +3σ (green) shows peaks close to carbonyl oxygen atoms involved in hydrogen bonds in the ß-sheet region (a) and the ɑ-helix region (b). There are fewer negative (−3σ pink) than positive (+3σ green) difference peaks. c, d Isomorphous difference density maps (F_obs(Δt)–F_{obs(single pulse)}) of thaumatin (c) and lysozyme.Gd (d) averaged over all peptide bonds shows also negative peaks (−3σ (red) and +3σ (green)). Both proteins show the effect, but it is less dependent on the delay time in case of lysozyme.Gd. This may be due to data quality; the lysozyme.Gd data deteriorate much faster than those of thaumatin (Supplementary Figs. 2–4, Supplementary Tables 1 and 2). e Refined bond lengths of the peptide bonds in lysozyme.Gd (blue filled symbols) and thaumatin (red filled symbols). The bond lengths are average values of 100 independently refined structures using a jackknife approach. The values of standard bond lengths⁶⁰ are displayed using open symbols.