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Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone

DOI: 10.1107/S2052252520015754 DOI Help

Authors: Thomas Zacharchenko (University of Leeds) , Stephanie Wright (University of Leeds)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Iucrj , VOL 8

State: Published (Approved)
Published: March 2021
Diamond Proposal Number(s): 15378 , 19248

Open Access Open Access

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.

Journal Keywords: protein crystallization; crystallization chaperone; BTB domain; porous crystal lattice

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Other Facilities: ID30A-1 at ESRF