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. 2020 Dec 4;11:6204. doi: 10.1038/s41467-020-20044-z

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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. 6 — a AlfC catalyzed transfer of fucose from α-fucosyl fluoride; and b IgG1 antibody (S0G2 glycoform). Separate reactions were measured with error bars representing standard deviation of n = 3 independent experiments. Data are presented as mean values ± SEM. c, d Hydrogen–deuterium exchange mass spectrometry analysis of transfucosylation mutants. Maximum differences in percent deuteration of peptides at 10 s or 1 min from c AlfC_E274A and d AlfC_N243A compared to wild-type. Differences are mapped onto a surface representation of AlfC bound to fucose (magenta). The site of mutation and the position of D242 are annotated with arrows. Source data are provided as a Source Data file.