Publication Date:
2012-06-28
Description:
The extracellular protein Epf fromStreptococcus pyogenesis important for streptococcal adhesion to human epithelial cells. However, Epf has no sequence identity to any protein of known structure or function. Thus, several predicted domains of the 205 kDa protein Epf were cloned separately and expressed inEscherichia coli. The N-terminal domain of Epf was crystallized in space groupsP21andP212121in the presence of the protease chymotrypsin. Mass spectrometry showed that the species crystallized corresponded to a fragment comprising residues 52–357 of Epf. Complete data sets were collected to 2.0 and 1.6 Å resolution, respectively, at the Australian Synchrotron.
Print ISSN:
1744-3091
Topics:
Biology
,
Chemistry and Pharmacology
,
Geosciences
,
Physics
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