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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. 2002 Sep; 58(Pt 9):1504-6.AC

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.

Authors+Show Affiliations

Park H
School of Molecular Biosciences, Washington State University, Pullman 99164-4660, USA.
Suquet C
No affiliation info available
Savenkova MI
No affiliation info available
Satterlee JD
No affiliation info available
Kang C
No affiliation info available

MeSH

Cloning, MolecularCrystallizationCrystallography, X-RayEscherichia coliHemeOxygenPlasmidsProtein ConformationSpectrophotometry, Ultraviolet

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

12198316

Citation

Park, HaJeung, et al. "Cloning, Purification, Crystallization and Preliminary X-ray Analysis of DOS Heme Domain, a New Heme Oxygen Sensor in Escherichia Coli." Acta Crystallographica. Section D, Biological Crystallography, vol. 58, no. Pt 9, 2002, pp. 1504-6.
Park H, Suquet C, Savenkova MI, et al. 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. 2002;58(Pt 9):1504-6.
Park, H., Suquet, C., Savenkova, M. I., Satterlee, J. D., & Kang, C. (2002). Cloning, purification, crystallization and preliminary X-ray analysis of DOS heme domain, a new heme oxygen sensor in Escherichia coli. Acta Crystallographica. Section D, Biological Crystallography, 58(Pt 9), 1504-6.
Park H, et al. 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. 2002;58(Pt 9):1504-6. PubMed PMID: 12198316.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cloning, purification, crystallization and preliminary X-ray analysis of DOS heme domain, a new heme oxygen sensor in Escherichia coli. AU - Park,HaJeung, AU - Suquet,Christine, AU - Savenkova,Marina I, AU - Satterlee,James D, AU - Kang,ChulHee, Y1 - 2002/08/23/ PY - 2002/05/06/received PY - 2002/07/03/accepted PY - 2002/8/29/pubmed PY - 2003/2/14/medline PY - 2002/8/29/entrez SP - 1504 EP - 6 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 58 IS - Pt 9 N2 - 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. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/12198316/Cloning_purification_crystallization_and_preliminary_X_ray_analysis_of_DOS_heme_domain_a_new_heme_oxygen_sensor_in_Escherichia_coli_ DB - PRIME DP - Unbound Medicine ER -