Abstract
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 Å resolution and belonged to the tetragonal space group P432 12, with unit-cell parameters a = 45.51, c = 84.26 Å. The asymmetric unit contains one protein molecule. © International Union of Crystallography 2008.
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Kounosu, A., Iwasaki, T., Baba, S., Hayashi-Iwasaki, Y., Oshima, T., & Kumasaka, T. (2008). Crystallization and preliminary X-ray diffraction studies of the prototypal homologue of mitoNEET (Tth-NEET0026) from the extreme thermophile Thermus thermophilus HB8. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 64(12), 1146–1148. https://doi.org/10.1107/S1744309108035975
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