Crystallization and preliminary X-ray diffraction analysis of the metalloregulatory protein DtxR from Thermoplasma acidophilum

Hyun Ku Yeo, Jina Kang, Young Woo Park, Jung Suk Sung, Jae Young Lee

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

The diphtheria toxin repressor (DtxR) is a metal-ion-dependent transcriptional regulator which regulates genes encoding proteins involved in metal-ion uptake to maintain metal-ion homeostasis. DtxR from Thermoplasma acidophilum was cloned and overexpressed in Escherichia coli. Crystals of N-terminally His-tagged DtxR were obtained by hanging-drop vapour diffusion and diffracted to 1.8 Å resolution. DtxR was crystallized at 296 K using polyethylene glycol 4000 as a precipitant. The crystals belonged to the orthorhombic space group P21212, with unit-cell parameters a = 61.14, b = 84.61, c = 46.91 Å, α = β = γ = 90°. The asymmetric unit contained approximately one monomer of DtxR, giving a crystal volume per mass (V M) of 2.22 Å 3 Da -1 and a solvent content of 44.6%.

Original languageEnglish
Pages (from-to)172-174
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume68
Issue number2
DOIs
StatePublished - Feb 2012

Keywords

  • DtxR
  • metalloregulatory proteins
  • Thermoplasma acidophilum
  • transcriptional regulators

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