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. 2020 Feb 14;11:899. doi: 10.1038/s41467-020-14754-7

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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 Hydrolytic activity of EndoBT-3987 and mutants against HM-IgG1 and RNaseB is shown, as determined by LC-MS analysis, normalized to EndoBT-3987_WT. Statistical significance compared with wild-type EndoBT is annotated (multiple comparisons test, Tukey method; *p < 0.05; **p < 0.01; ***p < 0.001, ****p < 0.0001, n.s. > 0, not significantly greater than no-enzyme control). Source data are provided as a ‘Source_Data_File_Fig_4a’. b In the left panel cartoon representation of the β-sandwich domain. The mutated residues are highlighted in oranges. In the right panel surface representation of the EndoBT-3987_D312A/E314L-Man₉GlcNAc₂Asn crystal structure showing the alanine mutations performed in loop 1 (yellow), loop 2 (orange), loop 3 (pink), loop 7 (brown), and loop 8 (gray) in the glycosidase domain (gray).