Expression, refolding and crystallization of the OpcA invasin from Neisseria meningitidis

Research output: Contribution to journalArticlepeer-review

  • External authors:
  • C. Feron
  • D. Janssens
  • Y. Lobet
  • M. Achtman
  • B. Kusecek
  • P. A. Bullough

Abstract

OpcA is an integral outer membrane from the Gram-negative pathogen Neisseria meningitidis that plays a role in adhesion of meningococci to host cells. The protein was overexpressed in Escherichia coli in an insoluble form and a procedure developed for refolding by rapid dilution from denaturant into detergent solution. The refolded material was identical to native OpcA isolated from meningococci, as judged by overall molecular weight, migration on SDS-PAGE and reaction against monoclonal antibodies. Both native and recombinant OpcA crystallized under similar conditions to give an orthorhombic crystal form (P21212), with unit-cell parameters a = 96.9, b = 46.3, c = 74.0 Å. Complete data sets of reflections were collected from native and refolded OpcA to 2.0 Å resolution.

Bibliographical metadata

Original languageEnglish
Pages (from-to)1164-1166
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number8
DOIs
Publication statusPublished - 2001