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-...

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

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