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  • Title: Crystallization and preliminary crystallographic analysis of the NheA component of the Nhe toxin from Bacillus cereus.
    Author: Phung D, Ganash M, Sedelnikova SE, Lindbäck T, Granum PE, Artymiuk PJ.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2012 Sep 01; 68(Pt 9):1073-6. PubMed ID: 22949198.
    Abstract:
    The nonhaemolytic enterotoxin (Nhe) of Bacillus cereus plays a key role in cases of B. cereus food poisoning. The toxin is comprised of three different proteins: NheA, NheB and NheC. Here, the expression in Escherichia coli, purification and crystallization of the NheA protein are reported. The protein was crystallized by the sitting-drop vapour-diffusion method using PEG 3350 as a precipitant. The crystals of NheA diffracted to 2.05 Å resolution and belonged to space group C2, with unit-cell parameters a = 308.7, b = 58.2, c = 172.9 Å, β = 110.6°. Calculation of V(M) values suggests that there are approximately eight protein molecules per asymmetric unit.
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