Crystallization of parasporin-2, a Bacillus thuringiensis crystal protein with selective cytocidal activity against human cells

Toshihiko Akiba, Yuichi Abe, Sakae Kitada, Yoshitomo Kusaka, Akio Ito, Tokio Ichimatsu, Hideki Katayama, Tetsuyuki Akao, Kazuhiko Higuchi, Eiichi Mizuki, Michio Ohba, Ryuta Kanai, Kazuaki Harata

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

Bacillus thuringiensis is a valuable source of protein toxins that are specifically effective against certain insects and worms but harmless to mammals. In contrast, a protein toxin obtained from B. thuringiensis strain A1547, designated parasporin-2, is not insecticidal but has a strong cytocidal activity against human cells with markedly divergent target specificity. The 37 kDa inactive protein is proteolytically activated to a 30 kDa active form. The active form of the recombinant protein toxin was crystallized in the presence of ethylene glycol and polyethylene glycol 8000 at neutral pH. The crystals belong to the hexagonal space group P61 or P65, with unit-cell parameters a = b = 134.37, c = 121.24 Å. Diffraction data from a native crystal were collected to 2.75 Å resolution using a synchrotron-radiation source.

Original languageEnglish
Pages (from-to)2355-2357
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number12 II
DOIs
Publication statusPublished - Dec 2004

All Science Journal Classification (ASJC) codes

  • Structural Biology

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