| Literature DB >> 22949198 |
Danh Phung1, Magdah Ganash, Svetlana E Sedelnikova, Toril Lindbäck, Per Einar Granum, Peter J Artymiuk.
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.Entities:
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Year: 2012 PMID： 22949198 PMCID： PMC3433201 DOI： 10.1107/S1744309112030813
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN： 1744-3091