Crystallization and preliminary X-ray diffraction analysis of tetrathionate hydrolase from Acidithiobacillus ferrooxidans

Tadayoshi Kanao, Megumi Kosaka, Kyoya Yoshida, Hisayuki Nakayama, Taro Tamada, Ryota Kuroki, Hidenori Yamada, Jun Takada, Kazuo Kamimura

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Tetrathionate hydrolase (4THase) from the iron- and sulfur-oxidizing bacterium Acidithiobacillus ferrooxidans catalyses the disproportionate hydrolysis of tetrathionate to elemental sulfur, thiosulfate and sulfate. The gene encoding 4THase (Af-tth) was expressed as inclusion bodies in recombinant Escherichia coli. Recombinant Af-Tth was activated by refolding under acidic conditions and was then purified to homogeneity. The recombinant protein was crystallized in 20 mM glycine buffer pH 10 containing 50 mM sodium chloride and 33%(v/v) PEG 1000 using the hanging-drop vapour-diffusion method. The crystal was a hexagonal cylinder with dimensions of 0.2 × 0.05 × 0.05 mm. X-ray crystallographic analysis showed that the crystal diffracted to 2.15 Å resolution and belongs to space group P31 or P32, with unit-cell parameters a = b = 92.1, c = 232.6 Å.

Original languageEnglish
Pages (from-to)692-694
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number6
DOIs
Publication statusPublished - Jun 10 2013

Keywords

  • Acidithiobacillus ferrooxidans
  • tetrathionate hydrolase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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