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.

The crystal structure of the aromatic-amino-acid aminotransferase from Streptococcus mutans was solved at 2.2 Å resolution by the molecular-replacement method.

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.

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.

The structure of the C-terminal domain of the S. mutans surface adhesin SpaP has been determined to 2.2 Å resolution.

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.

Crystals of FimP from A. oris were obtained. To facilitate selenomethionine labelling, three methionines were introduced by site-directed mutagenesis.

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.

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-NR_α, which is activated by acidic pH, has been crystallized at pH 5.0 and diffraction data have been collected to 3.0 Å resolution.

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.