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. 2017 Nov 15;7:15638. doi: 10.1038/s41598-017-15715-9

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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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Biochemical characterization of the N-terminal domain of CDC73 (CDC73-NTD). (a) Schematic representation of human CDC73 and CDC73 fragments used in this study. Full-length human CDC73 consists of 531 residues containing a nuclear localization signal (NLS) and a β-catenin interaction domain (CID). The dash line indicates the boundary of a protease-resistant fragment. (b) One trypsin-resistant fragment can be obtained through limited proteolysis of CDC73(1–343), which contains the first 111 residues of hCDC73 (CDC73-NTD). The marked ratios are the molar ratios of trypsin over hCDC73(1–343) used in limited proteolysis. The SDS-PAGE gel was stained with Coomassie Brilliant Blue. (c) Analytical ultracentrifugation (AUC) analysis demonstrates that CDC73(1–111) has a molecular weight of 11.9 kDa, which is close to the nominal MW of monomeric hCDC73(1–111) (12.7 kDa). The inlet shows the SDS-PAGE of our hCDC73(1–111) sample used for crystallographic and AUC analysis, stained with Coomassie Brilliant Blue.