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. 2018 Feb 8;8:2600. doi: 10.1038/s41598-018-20925-w

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© The Author(s) 2018

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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Mass spectrometry (MALDI-TOF/TOF) results indicate successful methylation of the PilN_Δ44/PilO_Δ51/PilP_Δ18 complex but only PilO fragments were present in the crystals. (A) Methylated (top) and unmethylated (bottom) samples of 1 mg/mL PilN_Δ44/PilO_Δ51/PilP_Δ18 was analyzed on a Bruker UltrafleXtreme linear detector in positive ion mode. The change in the molecular weight of PilN, PilO and PilP between the methylated and unmethylated samples were 319 Da, 313 Da, and 324 Da, respectively. All three protein fragments have 11 lysine residues, which could be methylated. A single dimethyl-Lys group adds 28 Da. (B) Two crystals were washed and resuspended in buffer and was analyzed on a Bruker UltrafleXtreme linear detector in positive ion mode. This weight corresponds to a 110–206 fragment of PilO (approximate molecular weight of 10,560 Da). Remaining peaks–were confirmed to be various PilO fragments. The numbers above the peaks are the molecular weights shown in Da. The chromatogram shows the ion intensities (in arbitrary units) according to mass-to-charge (m/z) ratio.