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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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| Materias: | |
| 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 |