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. 2024 Dec 23;15:10724. doi: 10.1038/s41467-024-54901-y

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© The Author(s) 2024

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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Fig. 3 — a Workflow for generation of the heterochiral d-Abl SH2:l-monobody complex. d-Abl SH2 was produced by solid-phase peptide synthesis (SPPS) and native chemical ligation (NCL) and the l-monobody by bacterial expression and subsequent purification. After mixing, the complex was purified by size exclusion chromatography (SEC). b, c Analytical SEC of complex formation between synthetic d-Abl SH2 and recombinantly expressed (b) l-DAM21 and (c) l-DAM27. d Preparative SEC of d-Abl SH2:l-monobody complexes generated for crystallization condition screening. All chromatograms include a calibration of the column with standard proteins on top. e Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the complex formation (performed once). Source data of (e) are provided as a Source Data file.