1. Expression, crystallization and preliminary X-ray diffraction studies of recombinant Clostridium perfringensβ2-toxin.
- Author
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Gurjar, Abhijit A., Yennawar, Neela H., Yennawar, Hemant P., Rajashankar, Kanagalaghatta R., Hegde, Narasimha V., and Jayarao, Bhushan M.
- Subjects
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CRYSTALLIZATION , *X-ray diffraction , *CLOSTRIDIUM perfringens , *CLOSTRIDIUM , *BACILLACEAE - Abstract
Clostridium perfringens is a Gram-positive sporulating anaerobic bacterium that is responsible for a wide spectrum of diseases in animals, birds and humans. The virulence of C. perfringens is associated with the production of several enterotoxins and exotoxins. β2-toxin is a 28 kDa exotoxin produced by C. perfringens. It is implicated in necrotic enteritis in animals and humans, a disease characterized by a sudden acute onset with lethal hemorrhagic mucosal ulceration. The recombinant expression, purification and crystallization of β2-toxin using the batch-under-oil technique are reported here. Native X-ray diffraction data were obtained to 2.9 Å resolution on a synchrotron beamline at the F2 station at Cornell High Energy Synchrotron Source (CHESS) using an ADSC Quantum-210 CCD detector. The crystals belong to space group R3, with a dimer in the asymmetric unit; the unit-cell parameters are a = b = 103.71, c = 193.48 Å, α = β = 90, γ = 120° using the hexagonal axis setting. A self-rotation function shows that the two molecules are related by a noncrystallographic twofold axis with polar angles ω = 90.0, ϕ = 210.3°. [ABSTRACT FROM AUTHOR]
- Published
- 2007
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