Purification, crystallization and preliminary X-ray analysis of an HA17-HA70 (HA2-HA3) complex from Clostridium botulinum type C progenitor toxin.

نویسندگان

  • Chikako Iwasa
  • Takashi Tonozuka
  • Masaya Shinoda
  • Yoshimasa Sagane
  • Koichi Niwa
  • Toshihiro Watanabe
  • Hiromi Yoshida
  • Shigehiro Kamitori
  • Toshifumi Takao
  • Keiji Oguma
  • Atsushi Nishikawa
چکیده

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(1)2(1)2. The molecular-replacement solution indicated that one molecule of HA17 was bound to each HA70 monomer.

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عنوان ژورنال:
  • Acta crystallographica. Section F, Structural biology communications

دوره 70 Pt 1  شماره 

صفحات  -

تاریخ انتشار 2014