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-...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
International Union of Crystallography
2021-03-01
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| Series: | IUCrJ |
| Subjects: | |
| Online Access: | http://scripts.iucr.org/cgi-bin/paper?S2052252520015754 |