TY - JOUR
T1 - Crystallization of parasporin-2, a Bacillus thuringiensis crystal protein with selective cytocidal activity against human cells
AU - Akiba, Toshihiko
AU - Abe, Yuichi
AU - Kitada, Sakae
AU - Kusaka, Yoshitomo
AU - Ito, Akio
AU - Ichimatsu, Tokio
AU - Katayama, Hideki
AU - Akao, Tetsuyuki
AU - Higuchi, Kazuhiko
AU - Mizuki, Eiichi
AU - Ohba, Michio
AU - Kanai, Ryuta
AU - Harata, Kazuaki
PY - 2004/12
Y1 - 2004/12
N2 - 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.
AB - 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.
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U2 - 10.1107/S0907444904026307
DO - 10.1107/S0907444904026307
M3 - Article
C2 - 15583389
AN - SCOPUS:21644480302
SN - 0907-4449
VL - 60
SP - 2355
EP - 2357
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
IS - 12 II
ER -