Abstract
The POU domain of the human Oct1 transcription factor has been crystallized with two different POU-dimer-binding DNA elements. Protein-DNA cocrystals suitable for structural analysis could be obtained only with a redox-insensitive version of the POU domain. The recombinant protein expression in a prokaryotic host was adjusted for fast purification. Optimized crystals were obtained by systematically varying the length of the oligonucleotide and by modifying cryofreezing procedures. These steps are generally applicable to the preparation of protein-DNA complexes for structural studies.
| Original language | English |
|---|---|
| Pages (from-to) | 1634-1638 |
| Number of pages | 5 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 57 |
| Issue number | 11 |
| DOIs | |
| Publication status | Published - 2001 |
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ASJC Scopus subject areas
- Clinical Biochemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
- Condensed Matter Physics
- Structural Biology
Cite this
Crystallization of redox-insensitive Oct1 POU domain with different DNA-response elements. / Reményi, A.; Pohl, E.; Schöler, H. R.; Wilmanns, M.
In: Acta Crystallographica Section D: Biological Crystallography, Vol. 57, No. 11, 2001, p. 1634-1638.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization of redox-insensitive Oct1 POU domain with different DNA-response elements
AU - Reményi, A.
AU - Pohl, E.
AU - Schöler, H. R.
AU - Wilmanns, M.
PY - 2001
Y1 - 2001
N2 - The POU domain of the human Oct1 transcription factor has been crystallized with two different POU-dimer-binding DNA elements. Protein-DNA cocrystals suitable for structural analysis could be obtained only with a redox-insensitive version of the POU domain. The recombinant protein expression in a prokaryotic host was adjusted for fast purification. Optimized crystals were obtained by systematically varying the length of the oligonucleotide and by modifying cryofreezing procedures. These steps are generally applicable to the preparation of protein-DNA complexes for structural studies.
AB - The POU domain of the human Oct1 transcription factor has been crystallized with two different POU-dimer-binding DNA elements. Protein-DNA cocrystals suitable for structural analysis could be obtained only with a redox-insensitive version of the POU domain. The recombinant protein expression in a prokaryotic host was adjusted for fast purification. Optimized crystals were obtained by systematically varying the length of the oligonucleotide and by modifying cryofreezing procedures. These steps are generally applicable to the preparation of protein-DNA complexes for structural studies.
UR - http://www.scopus.com/inward/record.url?scp=0034768606&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034768606&partnerID=8YFLogxK
U2 - 10.1107/S090744490101099X
DO - 10.1107/S090744490101099X
M3 - Article
C2 - 11679729
AN - SCOPUS:0034768606
VL - 57
SP - 1634
EP - 1638
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 0907-4449
IS - 11
ER -