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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. 3 — a The isomorphous difference electron density map (F_obs(18fs) – F_{obs(single pulse)})²⁹ of thaumatin shows peaks (−3σ (pink) and +3σ (green)) in the center of phenyl rings. In addition, there are changes around the adjacent elongated Cys145-Csy134 disulfide bridge and the backbone carbonyl oxygen atoms. b Averaged difference density (18 fs time delay point) of all phenylalanines (11), tyrosines (8) and tryptophan (3) side chain in thaumatin. c The difference electron density maps averaged over all phenylalanine residues shows that the negative difference is highest after 18 fs and no longer visible at 54 fs. It is unclear whether this latter observation is an effect of data quality.