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

Research output: Contribution to journalArticlepeer-review

  • External authors:
  • Muhammad Saleem
  • Hema Patel
  • Hannah Chan
  • Ian M. Feavers


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 homogeneity. Two separate antigenic variants of FrpB were crystallized by sitting-drop vapour diffusion. Crystals of the F5-1 variant diffracted to 2.4 Å resolution and belonged to space group C2, with unit-cell parameters a = 176.5, b = 79.4, c = 75.9 Å, β = 98.3°. Crystal-packing calculations suggested the presence of a monomer in the asymmetric unit. Crystals of the F3-3 variant also diffracted to 2.4 Å resolution and belonged to space group P212121, with unit-cell parameters a = 85.3, b = 104.6, c = 269.1 Å. Preliminary analysis suggested the presence of an FrpB trimer in the asymmetric unit. © 2012 International Union of Crystallography. All rights reserved.

Bibliographical metadata

Original languageEnglish
Pages (from-to)231-235
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number2
Publication statusPublished - Feb 2012