Open AccessCrystallization and preliminary X‐ray diffraction analysis of tetrathionate hydrolase from Acidithiobacillus ferrooxidans
Author(s) -
Kanao Tadayoshi,
Kosaka Megumi,
Yoshida Kyoya,
Nakayama Hisayuki,
Tamada Taro,
Kuroki Ryota,
Yamada Hidenori,
Takada Jun,
Kamimura Kazuo
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113013419
Subject(s) - tetrathionate , thiosulfate , chemistry , acidithiobacillus , crystallization , sulfur , nuclear chemistry , hydrolysis , biochemistry , organic chemistry , bioleaching , acidithiobacillus ferrooxidans , copper
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 m M glycine buffer pH 10 containing 50 m M 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 P 3 1 or P 3 2 , with unit‐cell parameters a = b = 92.1, c = 232.6 Å.