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Crystallization of the fimbrial protein FimP from Actinomyces oris and of a triple Ile-to-Met mutant engineered to facilitate selenomethionine labelling
Umeå University, Faculty of Medicine, Department of Odontology, Cariology. (Karina Persson)
2011 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. F67, 1207-1210 p.Article in journal (Refereed) Published
Abstract [en]

Actinomyces oris is an oral bacterium important for the development of dental plaque. It expresses two forms of fimbriae: type 1 and type 2. FimP, which is the fimbrial protein that is polymerized into the stalk of the type 1 fimbriae, was cloned, overexpressed and crystallized. X-ray data were collected and processed to 2.2 Å resolution. The crystals belonged to space group P21212, with one molecule in the asymmetric unit. To facilitate structure determination using single anomalous dispersion, three methionines were introduced by site-directed mutagenesis. Crystals of selenomethionine-labelled protein were obtained by streak-seeding and diffracted to 2.0 Å resolution.

Place, publisher, year, edition, pages
International Union of Crystallography , 2011. Vol. F67, 1207-1210 p.
Keyword [en]
protein crystals, fimbria, biofilms, mutagenesis
National Category
Structural Biology
Research subject
Molecular Biology; Odontology; Microbiology
URN: urn:nbn:se:umu:diva-49350DOI: 10.1107/S1744309111025929OAI: diva2:455304
Swedish Research Council
Available from: 2011-11-10 Created: 2011-11-09 Last updated: 2011-12-08Bibliographically approved

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