PMID:12198316

Citation	Park, H, Suquet, C, Savenkova, MI, Satterlee, JD and Kang, C (2002) Cloning, purification, crystallization and preliminary X-ray analysis of DOS heme domain, a new heme oxygen sensor in Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58:1504-6
Abstract	The heme-containing PAS domain of the direct oxygen-sensor protein (DOS(H)), a bona fide oxygen-sensor protein, has been cloned from Escherichia coli strain K12 and successfully purified. The oxidized form of this protein was crystallized by the hanging-drop method with a PEG 8000-based precipitant. Preliminary X-ray diffraction studies of the PAS-domain crystal show that it belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 46.1, b = 68.1, c = 82.6 A. A complete diffraction data set was collected to 1.9 A for MAD phasing. The electron-density map shows two molecules in an asymmetric unit and a unique six-coordination of the heme iron.
Links	PubMed Online version:10.1107/S0907444902011794
Keywords	Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Heme/chemistry; Oxygen/analysis; Plasmids; Protein Conformation; Spectrophotometry, Ultraviolet
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