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Search query: dental plaque
22 articles match your search "dental plaque"Results 1 to 10, sorted by relevance:
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The recombinant production and crystallization of the PitA adhesin from the Streptococcus oralis pilus island 2-encoded sortase-dependent pilus is described. Limited proteolysis of PitA and its complex with terbium crystallophore gave greatly improved X-ray diffraction to 2.16 Å resolution and a sufficiently strong anomalous signal for terbium SAD phasing, respectively.
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The crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans was solved at 2.2 Å resolution by the molecular-replacement method.
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The catalytic domain of α-1,3-glucanase FH1 from Paenibacillus glycanilyticus FH11, which may be of application in dental care and the development of fungal cell-wall lytic enzymes, was expressed and purified, and the protein was crystallized using the sitting-drop vapor-diffusion method. Diffraction data were collected to a resolution of 1.6 Å.
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A preliminary comparison between the trace metal distributions in diseased and healthy teeth suggests that Zn, Cu and Ni may play a role in the progression of periodontal disease.
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The structure of the C-terminal domain of the S. mutans surface adhesin SpaP has been determined to 2.2 Å resolution.
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Apo and acarbose-complex structures of the catalytic domain of GtfB from Streptococcus mutans and the truncated structure of the catalytic domain of GtfD are described.
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Crystals of FimP from A. oris were obtained. To facilitate selenomethionine labelling, three methionines were introduced by site-directed mutagenesis.
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In this study, the glucansucrase from the dental caries pathogen S. mutans was purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant.
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The adhesin fimbriae-associated protein 1 (Fap1) is a surface protein of Streptococcus parasanguinis FW213 and plays a major role in the formation of dental plaque in humans. Here, the adhesive domain Fap1-NRα, which is activated by acidic pH, has been crystallized at pH 5.0 and diffraction data have been collected to 3.0 Å resolution.
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The C-terminal domain of the S. gordonii surface protein SspB has been expressed, purified and crystallized. Diffraction data have been collected to 2.1 Å resolution.