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Expression, purification and preliminary X‐ray analysis of the Neisseria meningitidis outer membrane protein PorB
Author(s) -
Tanabe Mikio,
Iverson Tina M.
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109032333
Subject(s) - neisseria meningitidis , bacterial outer membrane , neisseriaceae , microbiology and biotechnology , neisseria , virology , neisseria gonorrhoeae , chemistry , biology , bacteria , escherichia coli , biochemistry , genetics , antibiotics , gene
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: C 222, R 32 and P 6 3 . The C 222 crystal form may contain either one or two PorB monomers in the asymmetric unit, while both the R 32 and P 6 3 crystal forms contained one PorB monomer in the asymmetric unit. Of the three, the P 6 3 crystal form had the best diffraction quality, yielding data extending to 2.3 Å resolution.

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