Crystallization and preliminary X-ray diffraction studies of the prototypal homologue of mitoNEET (Tth-NEET0026) from the extreme thermophile Thermus thermophilus HB8

被引:9
|
作者
Kounosu, Asako [1 ]
Iwasaki, Toshio [1 ]
Baba, Seiki [2 ]
Hayashi-Iwasaki, Yoko [3 ]
Oshima, Tairo [3 ]
Kumasaka, Takashi [2 ,4 ]
机构
[1] Nippon Med Sch, Dept Biochem & Mol Biol, Bunkyo Ku, Tokyo 1138602, Japan
[2] Japan Synchrotron Radiat Res Inst SPring 8 JASRI, Sayo, Hyogo 6795198, Japan
[3] Kyowa Kako Co, Inst Environm Microbiol, Tokyo 1940035, Japan
[4] SPring 8 Ctr, RIKEN, Sayo, Hyogo 6795148, Japan
关键词
D O I
10.1107/S1744309108035975
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
MitoNEET (a mammalian mitochondrial outer membrane protein) is a potential pharmacological and clinical target of the insulin-sensitizer pioglitazone. The thermophilic homologue of mitoNEET (TTHA0026) from Thermus thermophilus HB8 has been heterologously overproduced in Escherichia coli and purified as a water-soluble prototypal protein containing the mitoNEET-like [2Fe-2S] cluster. The resultant recombinant protein, named Tth-NEET0026, has been crystallized in its oxidized form by the hanging-drop vapour-diffusion method using 17%(w/v) polyethylene glycol 4000, 8.5%(v/v) 2-propanol, 15%(v/v) glycerol and 0.085 M HEPES-NaOH pH 7.2. The dark reddish crystals diffracted to 1.80 angstrom resolution and belonged to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = 45.51, c = 84.26 angstrom. The asymmetric unit contains one protein molecule.
引用
收藏
页码:1146 / 1148
页数:3
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