Expression, purification, crystallization and preliminary crystallographic analysis of a putative Clostridium difficile surface protein Cwp19
2011
Study of Clostridium difficile Protein Cwp19
publication
Evidence: moderate
Author Information
Author(s): Kirby Jonathan M., Thiyagarajan Nethaji, Roberts April K., Shone Clifford C., Acharya K. Ravi
Primary Institution: University of Bath
Hypothesis
Understanding the molecular structure of the Cwp19 protein from Clostridium difficile.
Conclusion
The Cwp19 protein was successfully expressed, purified, and crystallized, revealing its potential structure.
Supporting Evidence
- Cwp19 is a putatively surface-located protein from Clostridium difficile.
- The protein was crystallized and diffracted to 2 Å resolution.
- The crystal is estimated to contain two molecules of Cwp19 per asymmetric unit.
Takeaway
Scientists studied a protein from a germ that causes diarrhea, and they figured out how to grow it in the lab to learn more about it.
Methodology
The N-terminal domain of Cwp19 was expressed, purified, and crystallized using sitting-drop vapor-diffusion.
Limitations
The full-length protein exhibited degradation issues during purification.
Digital Object Identifier (DOI)
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