S. Borisova et al., CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE LEPIDOPTERAN-SPECIFIC INSECTICIDAL CRYSTAL PROTEIN CRYLA(A), Journal of Molecular Biology, 243(3), 1994, pp. 530-532
A trypsin-activated CrylA(a) protein from Bacillus thuringiensis has b
een purified and crystallized. Crystals belong to orthorhombic space g
roup P2(1)2(1)2(1), with cell dimensions a = 53.3, b = 111.3 and c = 1
54.7 Angstrom. The crystals diffract to at least 2.2 Angstrom resoluti
on and are suitable for X-ray structural analysis. They contain a sing
le molecule in the asymmetric unit.