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Crystallization of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae


Casutt, M S; Wendelspiess, S; Steuber, J; Fritz, G (2010). Crystallization of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 66(Pt 12):1677-1679.

Abstract

The Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from the human pathogen Vibrio cholerae couples the exergonic oxidation of NADH by membrane-bound quinone to Na+ translocation across the membrane. Na+-NQR consists of six different subunits (NqrA-NqrF) and contains a [2Fe-2S] cluster, a noncovalently bound FAD, a noncovalently bound riboflavin, two covalently bound FMNs and potentially Q8 as cofactors. Initial crystallization of the entire Na+-NQR complex was achieved by the sitting-drop method using a nanolitre dispenser. Optimization of the crystallization conditions yielded flat yellow-coloured crystals with dimensions of up to 200×80×20 µm. The crystals diffracted to 4.0 Å resolution and belonged to space group P2(1), with unit-cell parameters a=94, b=146, c=105 Å, α=γ=90, β=111°.

Abstract

The Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from the human pathogen Vibrio cholerae couples the exergonic oxidation of NADH by membrane-bound quinone to Na+ translocation across the membrane. Na+-NQR consists of six different subunits (NqrA-NqrF) and contains a [2Fe-2S] cluster, a noncovalently bound FAD, a noncovalently bound riboflavin, two covalently bound FMNs and potentially Q8 as cofactors. Initial crystallization of the entire Na+-NQR complex was achieved by the sitting-drop method using a nanolitre dispenser. Optimization of the crystallization conditions yielded flat yellow-coloured crystals with dimensions of up to 200×80×20 µm. The crystals diffracted to 4.0 Å resolution and belonged to space group P2(1), with unit-cell parameters a=94, b=146, c=105 Å, α=γ=90, β=111°.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:2010
Deposited On:26 Jan 2011 15:33
Last Modified:07 Dec 2017 06:14
Publisher:International Union of Crystallography/Blackwell
ISSN:1744-3091
Free access at:PubMed ID. An embargo period may apply.
Publisher DOI:https://doi.org/10.1107/S1744309110043125
PubMed ID:21139223

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