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

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

Acta Crystallographica Section F, 69(6), p.692 - 694, 2013/06

https://doi.org/10.1107/S1744309113013419

Tetrathionate hydrolase (4THase) from the iron- and sulfur-oxidizing bacterium catalyses the disproportionate hydrolysis of tetrathionate to elemental sulfur, thiosulfate and sulfate. The gene encoding 4THase () was expressed as inclusion bodies in recombinant . Recombinant -Tth was activated by refolding under acidic conditions and was then purified to homogeneity. The recombinant protein was crystallized in 20 m glycine buffer pH 10 containing 50 m sodium chloride and 33%() 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 resolution and belongs to space group 3 or 3, with unit-cell parameters = = 92.1, = 232.6 .