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Crystallization and preliminary X-ray diffraction studies of the prototypal homologue of mitoNEET (Tth-NEET0026) from the extreme thermophile Thermus thermophilus HB8.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2008 Dec 01; Vol. 64 (Pt 12), pp. 1146-8. Date of Electronic Publication: 2008 Nov 28. - Publication Year :
- 2008
-
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 A resolution and belonged to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = 45.51, c = 84.26 A. The asymmetric unit contains one protein molecule.
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 64
- Issue :
- Pt 12
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 19052371
- Full Text :
- https://doi.org/10.1107/S1744309108035975