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Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus.
Acta Crystallogr D Biol Crystallogr. 2004 Nov; 60(Pt 11):2076-7.AC

Abstract

A protein disulfide oxidoreductase from the thermophilic bacterium Aquifex aeolicus has been overexpressed in Escherichia coli and crystallized at 298 K using the hanging-drop vapour-diffusion method. Crystals belong to space group R32, with unit-cell parameters a = b = 161.1, c = 153.1 A. A complete data set has been collected to 2.4 A using synchrotron radiation. Packing-density considerations agree with the presence of 2-4 monomers in the asymmetric unit, with a corresponding solvent content of 66-32%.

Authors+Show Affiliations

D'Ambrosio K
Dipartimento di Chimica Biologica-Sezione Biostrutture and Istituto di Biostrutture e Bioimmagini-CNR, University of Naples Federico II, via Mezzocannone 16, 80134 Naples, Italy.
De Simone G
No affiliation info available
Pedone E
No affiliation info available
Rossi M
No affiliation info available
Bartolucci S
No affiliation info available
Pedone C
No affiliation info available

MeSH

BacteriaBacterial ProteinsCrystallizationCrystallography, X-RayNADH, NADPH Oxidoreductases

Pub Type(s)

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

Language

eng

PubMed ID

15502332

Citation

D'Ambrosio, Katia, et al. "Crystallization and Preliminary X-ray Diffraction Studies of a Protein Disulfide Oxidoreductase From Aquifex Aeolicus." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 11, 2004, pp. 2076-7.
D'Ambrosio K, De Simone G, Pedone E, et al. Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 11):2076-7.
D'Ambrosio, K., De Simone, G., Pedone, E., Rossi, M., Bartolucci, S., & Pedone, C. (2004). Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 11), 2076-7.
D'Ambrosio K, et al. Crystallization and Preliminary X-ray Diffraction Studies of a Protein Disulfide Oxidoreductase From Aquifex Aeolicus. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 11):2076-7. PubMed PMID: 15502332.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aquifex aeolicus. AU - D'Ambrosio,Katia, AU - De Simone,Giuseppina, AU - Pedone,Emilia, AU - Rossi,Mosè, AU - Bartolucci,Simonetta, AU - Pedone,Carlo, Y1 - 2004/10/20/ PY - 2004/07/13/received PY - 2004/09/10/accepted PY - 2004/10/27/pubmed PY - 2005/5/17/medline PY - 2004/10/27/entrez SP - 2076 EP - 7 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 11 N2 - A protein disulfide oxidoreductase from the thermophilic bacterium Aquifex aeolicus has been overexpressed in Escherichia coli and crystallized at 298 K using the hanging-drop vapour-diffusion method. Crystals belong to space group R32, with unit-cell parameters a = b = 161.1, c = 153.1 A. A complete data set has been collected to 2.4 A using synchrotron radiation. Packing-density considerations agree with the presence of 2-4 monomers in the asymmetric unit, with a corresponding solvent content of 66-32%. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15502332/Crystallization_and_preliminary_X_ray_diffraction_studies_of_a_protein_disulfide_oxidoreductase_from_Aquifex_aeolicus_ DB - PRIME DP - Unbound Medicine ER -