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Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase.
Acta Crystallogr D Biol Crystallogr. 2004 Apr; 60(Pt 4):743-5.AC

Abstract

Transhydrogenase is a proton-pumping membrane protein that is required for the cellular regeneration of NADPH. The NAD(H)-binding domain (domain I) of transhydrogenase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique at room temperature. The crystals, which were grown from PEG 4000 and ammonium acetate in citrate buffer, belong to the triclinic space group P1, with unit-cell parameters a = 38.8, b = 66.8, c = 76.4 A, alpha = 67.5, beta = 80.8, gamma = 81.5 degrees. X-ray diffraction data were collected to 1.9 A resolution using synchrotron radiation. The crystals contain one dimer of transhydrogenase domain I per asymmetric unit.

Authors+Show Affiliations

Oswald C
Department of Chemistry and Bioscience, Chalmers University of Technology, PO Box 462, SE-405 30 Göteborg, Sweden.
Johansson T
No affiliation info available
Törnroth S
No affiliation info available
Okvist M
No affiliation info available
Krengel U
No affiliation info available

MeSH

Binding SitesCloning, MolecularCrystallizationCrystallography, X-RayEscherichia coli ProteinsNADNADP Transhydrogenases

Pub Type(s)

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

Language

eng

PubMed ID

15039572

Citation

Oswald, Christine, et al. "Crystallization and Preliminary Crystallographic Analysis of the NAD(H)-binding Domain of Escherichia Coli Transhydrogenase." Acta Crystallographica. Section D, Biological Crystallography, vol. 60, no. Pt 4, 2004, pp. 743-5.
Oswald C, Johansson T, Törnroth S, et al. Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 4):743-5.
Oswald, C., Johansson, T., Törnroth, S., Okvist, M., & Krengel, U. (2004). Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase. Acta Crystallographica. Section D, Biological Crystallography, 60(Pt 4), 743-5.
Oswald C, et al. Crystallization and Preliminary Crystallographic Analysis of the NAD(H)-binding Domain of Escherichia Coli Transhydrogenase. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 4):743-5. PubMed PMID: 15039572.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystallization and preliminary crystallographic analysis of the NAD(H)-binding domain of Escherichia coli transhydrogenase. AU - Oswald,Christine, AU - Johansson,Tomas, AU - Törnroth,Susanna, AU - Okvist,Mats, AU - Krengel,Ute, Y1 - 2004/03/23/ PY - 2003/12/19/received PY - 2004/01/28/accepted PY - 2004/3/25/pubmed PY - 2004/12/16/medline PY - 2004/3/25/entrez SP - 743 EP - 5 JF - Acta crystallographica. Section D, Biological crystallography JO - Acta Crystallogr D Biol Crystallogr VL - 60 IS - Pt 4 N2 - Transhydrogenase is a proton-pumping membrane protein that is required for the cellular regeneration of NADPH. The NAD(H)-binding domain (domain I) of transhydrogenase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique at room temperature. The crystals, which were grown from PEG 4000 and ammonium acetate in citrate buffer, belong to the triclinic space group P1, with unit-cell parameters a = 38.8, b = 66.8, c = 76.4 A, alpha = 67.5, beta = 80.8, gamma = 81.5 degrees. X-ray diffraction data were collected to 1.9 A resolution using synchrotron radiation. The crystals contain one dimer of transhydrogenase domain I per asymmetric unit. SN - 0907-4449 UR - https://www.unboundmedicine.com/medline/citation/15039572/Crystallization_and_preliminary_crystallographic_analysis_of_the_NAD_H__binding_domain_of_Escherichia_coli_transhydrogenase_ DB - PRIME DP - Unbound Medicine ER -