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Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):71-4. doi: 10.1107/S2053230X1402559X. Epub 2015 Jan 1.

Crystallization and preliminary X-ray analysis of the C-terminal fragment of PorM, a subunit of the Porphyromonas gingivalis type IX secretion system.

Author information

1
Architecture et Fonction des Macromolécules Biologiques (AFMB), UMR 7257 CNRS et Aix-Marseille Université, Marseille, France.
2
Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM), UMR 7255 CNRS et Aix-Marseille Université, Marseille, France.

Abstract

PorM is a membrane protein involved in the assembly of the type IX secretion system (T9SS) from Porphyromonas gingivalis, a major bacterial pathogen responsible for periodontal disease in humans. The periplasmic domain of PorM was overexpressed in Escherichia coli and purified. A fragment of the purified protein was obtained by limited proteolysis. Crystals of this fragment belonged to the tetragonal space group P4(3)2(1)2. Native and MAD data sets were recorded to 2.85 and 3.1 Å resolution, respectively, using synchrotron radiation.

KEYWORDS:

Porphyromonas gingivalis; T9SS

PMID:
25615973
PMCID:
PMC4304752
DOI:
10.1107/S2053230X1402559X
[Indexed for MEDLINE]
Free PMC Article

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