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. 2018 Jun 12;8:8948. doi: 10.1038/s41598-018-27051-7

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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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(A) Size exclusion chromatogram of mtbMGL after purification via Ni-NTA Agarose resin. The monomeric fraction (eluting at approximately 205 ml) was used for crystallization. (B) Asymmetric unit in the mtbMGL crystal. (C) Overall structure of mtbMGL (chain B), the cap region is in green and the α/β hydrolase core in wheat. The gray blob represents the cavity inside the protein calculated by CASOX. The small cavity accommodating the glycerol moiety is marked with a red circle. (D) Cap region of mtbMGL viewed from the top (compared to orientation in 1C). (E) Cap regions from hMGL and mtbMGL aligned to each other (hMGL in pink, mtbMGL in green. (F) Close up view on the active site of mtbMGL with the residues of the catalytic triad and the residues that build up the oxyanion hole shown as sticks.