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. 2018 Sep 18;9:3795. doi: 10.1038/s41467-018-06237-7

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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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Fig. 1 — Crystal structure of the human CTR9/PAF1 heterodimer. a Schematic representation of full-length CTR9 and PAF1. A LEO1-interacting region (blue) and a histone H3-interacting region (orange) are shown in PAF1. The predicted 19 TPR motifs (gray) were defined using TPRpred (https://toolkit.tuebingen.mpg.de/#/tools/tprpred). The protein fragments of the CTR9^(1–249)/PAF1^(57–116) complex used for structural determination are indicated by a two-way arrow and are colored cyan and magenta, respectively. b Ribbon diagram representation of the CTR9^(1–249) (cyan)/PAF1^(57–116) (magenta) complex viewed from the side. The N- and C-termini of the two proteins are labeled. Cylinder representation of the CTR9^(1–249)/PAF1^(57–116) complex structure viewed from the top (c) or the bottom (d). e Surface representation of the CTR9^(1–249)/PAF1^(57–116) complex with its orientation corresponding to the other side from that shown in (b)