Abstract
A recombinant form of a collagen-binding fragment of Yersinia enterocolitica serotype 0:3 adhesin YadA with an N-terminal polyhistidine affinity tag has been produced in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the trigonal space group R3, with unit-cell parameters a = b = 67.05, c = 221.95 Å, and diffract to 1.55 Å resolution on a synchrotron-radiation source.
| Original language | English |
|---|---|
| Pages (from-to) | 1042-1044 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 58 |
| Issue number | 6 II |
| DOIs | |
| Publication status | Published - 2002 |
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ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Clinical Biochemistry
- Structural Biology
- Condensed Matter Physics
Cite this
Nummelin, H., El Tahir, Y., Ollikka, P., Skurnik, M., & Goldman, A. (2002). Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA. Acta Crystallographica Section D: Biological Crystallography, 58(6 II), 1042-1044. https://doi.org/10.1107/S0907444902005231