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.
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|Issue number||12 II|
|Publication status||Published - Dec 2004|
All Science Journal Classification (ASJC) codes
- Structural Biology