Crystallization of redox-insensitive Oct1 POU domain with different DNA-response elements

A. Reményi, E. Pohl, H. R. Schöler, M. Wilmanns

Research output: Article

9 Citations (Scopus)

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 languageEnglish
Pages (from-to)1634-1638
Number of pages5
JournalActa Crystallographica Section D: Biological Crystallography
Volume57
Issue number11
DOIs
Publication statusPublished - 2001

Fingerprint

Response Elements
Crystallization
Oxidation-Reduction
deoxyribonucleic acid
crystallization
proteins
DNA
oligonucleotides
Recombinant Proteins
structural analysis
purification
Structural analysis
Oligonucleotides
Dimers
Purification
Proteins
Transcription Factors
dimers
preparation
Crystals

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: Article

@article{0d1695e1832e44729c832b4e9a0b6c3a,
title = "Crystallization of redox-insensitive Oct1 POU domain with different DNA-response elements",
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.",
author = "A. Rem{\'e}nyi and E. Pohl and Sch{\"o}ler, {H. R.} and M. Wilmanns",
year = "2001",
doi = "10.1107/S090744490101099X",
language = "English",
volume = "57",
pages = "1634--1638",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "11",

}

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 -