Open AccessCrystallization of the Na + ‐translocating NADH:quinone oxidoreductase from Vibrio cholerae
Author(s) -
Casutt Marco S.,
Wendelspiess Severin,
Steuber Julia,
Fritz Günter
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110043125
Subject(s) - crystallization , vibrio cholerae , quinone , oxidoreductase , crystallography , chemistry , cofactor , stereochemistry , biology , biochemistry , enzyme , bacteria , organic chemistry , genetics
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 Q 8 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 P 2 1 , with unit‐cell parameters a = 94, b = 146, c = 105 Å, α = γ = 90, β = 111°.