Purification, crystallization and preliminary X‐ray analysis of an HA17–HA70 (HA2–HA3) complex from Clostridium botulinum type C progenitor toxin. Issue 1 (1st January 2014)

• Record Type: Journal Article
• Authors: Iwasa, Chikako; Tonozuka, Takashi; Shinoda, Masaya; Sagane, Yoshimasa; Niwa, Koichi; Watanabe, Toshihiro; Yoshida, Hiromi; Kamitori, Shigehiro; Takao, Toshifumi; Oguma, Keiji; Nishikawa, Atsushi
• Is Part Of: Acta crystallographica. Volume 70:Issue 1(2014:Jan.)
• Page Start: 64
• Page End: 67
• Publication Date: 2014-01-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X13032378
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The haemagglutinin (HA) complex of <italic>Clostridium botulinum</italic> 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 <italic>Escherichia coli</italic> 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 <italic>P</italic>4₁2₁2. The molecular‐replacement solution indicated that one molecule of HA17 was bound to each HA70 monomer.</p> </abstract>