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Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2355-7. Epub 2004 Nov 26.

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

Author information

1
Biological Information Research Center, AIST, Tsukuba, Ibaraki 305-8566, Japan.

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 P6(1) or P6(5), with unit-cell parameters a = b = 134.37, c = 121.24 A. Diffraction data from a native crystal were collected to 2.75 A resolution using a synchrotron-radiation source.

PMID:
15583389
DOI:
10.1107/S0907444904026307
[Indexed for MEDLINE]

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