Zacharchenko, T and Wright, S orcid.org/0000-0002-3509-7506 (2021) Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone. IUCrJ, 8 (2). pp. 154-160. ISSN 2052-2525
Abstract
The production of diffraction-quality protein crystals is challenging and often requires bespoke, time-consuming and expensive strategies. A system has been developed in which the BCL6 BTB domain acts as a crystallization chaperone and promiscuous assembly block that may form the basis for affinity-capture crystallography. The protein of interest is expressed with a C-terminal tag that interacts with the BTB domain, and co-crystallization leads to its incorporation within a BTB-domain lattice. This strategy was used to solve the structure of the SH3 domain of human nebulin, a structure previously solved by NMR, at 1.56 Å resolution. This approach is simple and effective, requiring only routine protein complexation and crystallization screening, and should be applicable to a range of proteins.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © Zacharchenko & Wright 2021. This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
Keywords: | protein crystallization; crystallization chaperone; BTB domain; porous crystal lattice |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biology (Leeds) |
Funding Information: | Funder Grant number Kay Kendall Leukaemia Fund KK1047 |
Depositing User: | Symplectic Publications |
Date Deposited: | 04 Dec 2020 12:53 |
Last Modified: | 25 Jun 2023 22:31 |
Status: | Published |
Publisher: | International Union of Crystallography |
Identification Number: | 10.1107/S2052252520015754 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:168680 |