Crystallization and preliminary crystallographic analysis of the NheA component of the Nhe toxin from
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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Document Type: Research Article
Publication date: September 1, 2012