Volume 65, Issue 10 pp. 996-1000

Expression, purification and preliminary X-ray analysis of the Neisseria meningitidis outer membrane protein PorB

First published: 22 October 2009
Citations: 1
Tina M. Iverson, e-mail: [email protected]

Abstract

The Neisseria meningitidis outer membrane protein PorB was expressed in Escherichia coli and purified from inclusion bodies by denaturation in urea followed by refolding in buffered LDAO on a size-exclusion column. PorB has been crystallized in three different crystal forms: C222, R32 and P63. The C222 crystal form may contain either one or two PorB monomers in the asymmetric unit, while both the R32 and P63 crystal forms contained one PorB monomer in the asymmetric unit. Of the three, the P63 crystal form had the best diffraction quality, yielding data extending to 2.3 Å resolution.

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