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Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone
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-...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7924223/ https://www.ncbi.nlm.nih.gov/pubmed/33708392 http://dx.doi.org/10.1107/S2052252520015754 |
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author | Zacharchenko, Thomas Wright, Stephanie |
author_facet | Zacharchenko, Thomas Wright, Stephanie |
author_sort | Zacharchenko, Thomas |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7924223 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-79242232021-03-10 Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone Zacharchenko, Thomas Wright, Stephanie IUCrJ Research Letters 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. International Union of Crystallography 2021-01-11 /pmc/articles/PMC7924223/ /pubmed/33708392 http://dx.doi.org/10.1107/S2052252520015754 Text en © Zacharchenko & Wright 2021 http://creativecommons.org/licenses/by/4.0/ 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.http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Research Letters Zacharchenko, Thomas Wright, Stephanie Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone |
title | Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone |
title_full | Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone |
title_fullStr | Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone |
title_full_unstemmed | Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone |
title_short | Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone |
title_sort | functionalization of the bcl6 btb domain into a noncovalent crystallization chaperone |
topic | Research Letters |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7924223/ https://www.ncbi.nlm.nih.gov/pubmed/33708392 http://dx.doi.org/10.1107/S2052252520015754 |
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