6XWF
Crystal structure of an NCoR1BBD2-BCL6BTB chimera
Summary for 6XWF
| Entry DOI | 10.2210/pdb6xwf/pdb |
| Descriptor | B-cell lymphoma 6 protein, (4S)-2-METHYL-2,4-PENTANEDIOL, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | bcl6, ncor1., transcription |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15642.50 |
| Authors | Zacharchenko, T.,Wright, S.C. (deposition date: 2020-01-23, release date: 2020-12-02, Last modification date: 2024-01-24) |
| Primary citation | Zacharchenko, T.,Wright, S. Functionalization of the BCL6 BTB domain into a noncovalent crystallization chaperone. Iucrj, 8:154-160, 2021 Cited by PubMed 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. PubMed: 33708392DOI: 10.1107/S2052252520015754 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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