Crystallization and preliminary X‐ray analysis of the C‐terminal fragment of PorM, a subunit of the Porphyromonas gingivalis type IX secretion system. Issue 1 (1st January 2015)

• Record Type: Journal Article
• Authors: Stathopulos, Julien; Cambillau, Christian; Cascales, Eric; Roussel, Alain; Leone, Philippe
• Is Part Of: Acta crystallographica. Volume 71:Issue 1(2015:Jan.)
• Page Start: 71
• Page End: 74
• Publication Date: 2015-01-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X1402559X
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>PorM is a membrane protein involved in the assembly of the type IX secretion system (T9SS) from <italic>Porphyromonas gingivalis</italic>, a major bacterial pathogen responsible for periodontal disease in humans. The periplasmic domain of PorM was overexpressed in <italic>Escherichia coli</italic> and purified. A fragment of the purified protein was obtained by limited proteolysis. Crystals of this fragment belonged to the tetragonal space group <italic>P</italic>4₃2₁2. Native and MAD data sets were recorded to 2.85 and 3.1 Å resolution, respectively, using synchrotron radiation.</p> </abstract>