title: Crystallization and preliminary crystallographic analysis of the NheA component of the Nhe toxin from Bacillus cereus.
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.
authors.affiliation: Department of Food Safety and Infection Biology, Norwegian School of Veterinary Science, P.O. Box 8146 Dep, 0033 Oslo, Norway.
authors.forename: Danh
authors.initials: D
authors.lastname: Phung
authors.forename: Magdah
authors.initials: M
authors.lastname: Ganash
authors.forename: Svetlana E
authors.initials: SE
authors.lastname: Sedelnikova
authors.forename: Toril
authors.initials: T
authors.lastname: Lindbäck
authors.forename: Per Einar
authors.initials: PE
authors.lastname: Granum
authors.forename: Peter J
authors.initials: PJ
authors.lastname: Artymiuk
mesh_terms: D001409:Bacillus cereus / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004768:Enterotoxins / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D004768:Enterotoxins