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
Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA. / Nummelin, Heli; El Tahir, Yasmin; Ollikka, Pauli; Skurnik, Mikael; Goldman, Adrian.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 58, No. 6 II, 2002, p. 1042-1044.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Expression, purification and crystallization of a collagen-binding fragment of Yersinia adhesin YadA
AU - Nummelin, Heli
AU - El Tahir, Yasmin
AU - Ollikka, Pauli
AU - Skurnik, Mikael
AU - Goldman, Adrian
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0036618133&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036618133&partnerID=8YFLogxK
U2 - 10.1107/S0907444902005231
DO - 10.1107/S0907444902005231
M3 - Article
C2 - 12037311
AN - SCOPUS:0036618133
VL - 58
SP - 1042
EP - 1044
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 6 II
ER -