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. 2017 Aug 11;7:7913. doi: 10.1038/s41598-017-08489-7

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© The Author(s) 2017

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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MS analyses of LprG and LprG T231A glycosylation. (A) Deconvoluted ESI-HRMS spectrum of the purified recombinant LprG-His expressed in M. tuberculosis. (B) Peptide sequence of the molecular species observed in A reporting the fragment ions detected in the top-down electron transfer dissociation spectrum of the fragmentation of the 22,541 Da molecular mass ion precursor allowing the localization of the unique hexose on the T231. (C) Deconvoluted ESI-HRMS spectrum of purified recombinant LprG-His T231A expressed in M. smegmatis demonstrating the absence of glycosylation of the mutated protein. (D) Peptide sequence of the molecular species observed in C.