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. 2023 Apr 26;617(7959):176–184. doi: 10.1038/s41586-023-05993-x

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© The Author(s) 2023

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Extended Data Fig. 6 — a, Competition between designed binders and a known protein binder (native binder or monoclonal Fab) in complex with the target structure. b, Flow cytometry histograms showing fluorescence signals on the surface of yeast displaying the different binders. Yeasts were labelled with 500 nM or their respective ligand (blue), 500 nM of blocked ligand pre-incubated with 10-fold molar excess of Fab or high-affinity PD-1 (HA-PD-1) (orange) or labelled with secondary antibodies only (grey, Neg Ctrl). c, Flow cytometry histograms showing fluorescence signal on the surface of yeast displaying the different binders and labelled with 500 nM of unrelated protein ligand (red) or labelled with secondary antibodies only (grey, Neg Ctrl).