Crystallization of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae.
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°.
Department of Neuropathology, University of Freiburg, Breisacher Strasse 64, 79106 Freiburg, Germany.
Marco S
MS
Casutt
Severin
S
Wendelspiess
Julia
J
Steuber
Günter
G
Fritz
D001692:Biological Transport; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D011808:Quinone Reductases / Q000737:chemistry* / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism*; D014734:Vibrio cholerae / Q000201:enzymology*
D012964:Sodium; C041831:NADH dehydrogenase (quinone); D011808:Quinone Reductases