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Crystallization and preliminary X-ray diffraction analysis of tetrathionate hydrolase from ${it Acidithiobacillus ferrooxidans}$

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

Tetrathionate hydrolase (4THase) from the iron- and sulfur-oxidizing bacterium ${it Acidithiobacillus ferrooxidans}$ catalyses the disproportionate hydrolysis of tetrathionate to elemental sulfur, thiosulfate and sulfate. The gene encoding 4THase (${it Af-tth}$) was expressed as inclusion bodies in recombinant ${it Escherichia coli}$. Recombinant ${it Af}$-Tth was activated by refolding under acidic conditions and was then purified to homogeneity. The recombinant protein was crystallized in 20 m${it M}$ glycine buffer pH 10 containing 50 m${it M}$ sodium chloride and 33%(${it v/v}$) PEG 1000 using the hanging-drop vapour-diffusion method. The crystal was a hexagonal cylinder with dimensions of 0.2 $$times$$ 0.05 $$times$$ 0.05 mm. X-ray crystallographic analysis showed that the crystal diffracted to 2.15 ${AA}$ resolution and belongs to space group ${it P}$3$$_{1}$$ or ${it P}$3$$_{2}$$, with unit-cell parameters ${it a}$ = ${it b}$ = 92.1, ${it c}$ = 232.6 ${AA}$.

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Category:Biochemical Research Methods

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