Expression, purification, and co-crystallization of IRF-I bound to the interferon-β element PRDI

Carlos R. Escalante, Junming Yie, Dimitris Thanos, Aneel K. Aggarwal

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Interferon regulatory factor 1 (IRF-1) is an essential factor involved in the regulation of type I interferon (IFN) and IFN-inducible genes. The protein consists of 329 amino acids that are highly conserved from mouse to human. Similar to other transcription factors, the protein is modular in nature with a basic N-terminal region inolved in DNA binding and an acidic C-terminal region required for activation. We report here the expression, purification and co-crystallization of the minimal N-terminal region of IRF-I involved in DNA binding (amino acids 1-113) with a 13 bp DNA fragment from the IFN-β promoter. The crystals diffract to at least 3.0 Å in resolution and belong to space group R3 with unit cell parameters of a = b = 84.8 Å, c = 203.7 Å.

Original languageEnglish
Pages (from-to)219-220
Number of pages2
JournalFEBS Letters
Volume414
Issue number2
DOIs
StatePublished - 8 Sep 1997

Keywords

  • DNA-binding protein
  • Interferon
  • Transcription factor
  • X-ray crystallography

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