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. 2019 Jan 30;9:987. doi: 10.1038/s41598-018-37699-w

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© The Author(s) 2019

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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SANT1 is a histone reader domain specific for the H4 tail. (a) ¹H-¹⁵N HSQC overlay of SRM-SANT1 in the presence of increasing concentrations of H2A (1–20, red), H2B (1–11, green), H3 (1–21, orange), H3 (21–44, orange) and H4 (1–21, blue). Molar ratio of ligand added is indicated in the legend. (b–d) All binding curves used to calculate the K_d for (b) H2A (1–20) peptide, (c) H2B (1–11) peptide, or (d) H4 (1–21) peptide. (e) Table of K_ds for all histone tail peptides tested. Underdetermined K_d values due to lack of saturation are given as lower limits, the H4 value is the average over all significant CSPs and associated standard deviation, NB is no binding.