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. 2013 Sep 14;41(22):10619–10629. doi: 10.1093/nar/gkt819

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© The Author(s) 2013. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 1. — Crystal structure of the human Paf1/Leo1 subcomplex. (A and B) Gel filtration-based test of the binding of Paf1 and Leo1 by the co-expression of target proteins. ‘+’ indicates protein binding, according to the supporting data in Supplementary Figures S1 and S2; ‘−’ indicates no protein binding. The protein fragments of the complex used for structural determination were Paf1^(161–250) colored in cyan, and Leo1^(370–462) colored in magenta. (C) A cartoon representation of the structure of the Paf1^(161–250)-Leo1^(370–462) heterodimer complex. Paf1 is shown in cyan, and Leo1 is shown in magenta. The bound AdoMet is shown as a stick model and colored in yellow. (D) A side view of the Paf1^(161–250)-Leo1^(370–462) heterodimer complex. The N- and C-termini of the two proteins are labeled. For clarity, the β-strand formed by the artificial linker is not shown.