Refolding, purification and crystallization of the FrpB outer membrane iron transporter from Neisseria meningitidis.

@article{Saleem2012RefoldingPA,
  title={Refolding, purification and crystallization of the FrpB outer membrane iron transporter from Neisseria meningitidis.},
  author={Muhammad Saleem and Stephen M. Prince and Hema Patel and Hannah Chan and Ian M. Feavers and Jeremy P Derrick},
  journal={Acta crystallographica. Section F, Structural biology and crystallization communications},
  year={2012},
  volume={68 Pt 2},
  pages={231-5}
}
FrpB is an integral outer membrane protein from the human pathogen Neisseria meningitidis. It is a member of the TonB-dependent transporter family and promotes the uptake of iron across the outer membrane. There is also evidence that FrpB is an antigen and hence a potential component of a vaccine against meningococcal meningitis. FrpB incorporating a polyhistidine tag was overexpressed in Escherichia coli into inclusion bodies. The protein was then solubilized in urea, refolded and purified to… CONTINUE READING