The haemagglutinin (HA) complex of Clostridium botulinum type C toxin is composed of three types of subcomponents: HA33, HA17 and HA70 (also known as HA1, HA2 and HA3, respectively). Here, a 260 kDa HA17-HA70 complex was crystallized. His-tagged HA17 and maltose-binding-protein-tagged HA70 were expressed in Escherichia coli and their complex was affinity-purified using a combination of amylose resin chromatography and nickel-nitrilotriacetic acid agarose chromatography. Diffraction data were collected to 8.0 Å resolution and the crystal belonged to the tetragonal space group P4 1212. The molecular-replacement solution indicated that one molecule of HA17 was bound to each HA70 monomer. © 2014 International Union of Crystallography. All rights reserved.
CITATION STYLE
Iwasa, C., Tonozuka, T., Shinoda, M., Sagane, Y., Niwa, K., Watanabe, T., … Nishikawa, A. (2014). Purification, crystallization and preliminary X-ray analysis of an HA17-HA70 (HA2-HA3) complex from Clostridium botulinum type C progenitor toxin. Acta Crystallographica Section F:Structural Biology Communications, 70(1), 64–67. https://doi.org/10.1107/S2053230X13032378
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