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. 2019 Jul 9;9:9896. doi: 10.1038/s41598-019-45885-7

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© The Author(s) 2019

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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Closer view on the DNA binding site of CraCRY. For that the relative uptake of the FAD_OX state at 10 s was mapped onto the CraCRY∆CTE-DNA structure (PDB entry: 6FN0). (a) Here, the (6-4) damaged DNA (blue) is bound to the enzyme and the two catalytic histidines (green) are shown. (b) Q291 and K237 play a crucial role in DNA binding and are highly conserved (marked with *) as shown in the WebLogo that was generated from a multiple sequence alignment of animal-like cryptochromes⁸. Both residues are located on a stretch with high deuterium uptake in the WT. (c) The overall binding mode of the dsDNA is expected to be unaffected between CraCRY-WT and CraCRY∆CTE when taking the HDX analysis results without DNA into account.