EC Number   |
|---|
    1.3.5.1 | - |
| 1.3.5.1 | by the hanging-drop vapour-diffusion technique |
| 1.3.5.1 | crystal structure of QFR to 3.3 A resolution. Enzyme contains two quinone species, presumably menaquinol, bound to the transmembrane-spanning region. The binding sites for the two quinone molecules are termed QP and QD, indicating their positions proximal, QP, or distal, QD, to the site of fumarate reduction in the hydrophilic flavoprotein and iron-sulfur protein subunits. Co-crystallization studies of the Escherichia coli QFR with the quinol-binding site inhibitors 2-heptyl-4-hydroxyquinoline-N-oxide and 2-[1-(p-chlorophenyl)ethyl] 4,6-dinitrophenol establish that both inhibitors block the binding of MQH2 at the QP site. In the structures with the inhibitor bound at QP, no density is observed at QD. The conserved acidic residue, Glu29 in subunit FrdC, in the Escherichia coli enzyme may act as a proton shuttle from the quinol during enzyme turnover |
| 1.3.5.1 | crystallization conditions are screened for succinate-quinone oxidoreductase that is solubilized and purified using 2.5% (w/v) sucrose monolaurate and 0.5% (w/v) Lubrol PX, respectively, and two different crystal forms are obtained in the presence of detergent mixtures composed of n-alkyl-oligoethylene glycol monoether and n-alkyl-maltoside. Crystallization takes place before detergent phase separation occurrs and the type of detergent mixture affects the crystal form |
| 1.3.5.1 | fumarate reductase, determined at 3.3 A, belongs to the type D enzymes: contains two hydrophobic subunits and no heme group |
| 1.3.5.1 | fumarate reductase, refined at 2.2-A resolution, belongs to the type B enzymes: contains one hydrophobic subunit and two heme groups |
| 1.3.5.1 | hanging drop method, crystal structure of complex II from porcine heart at 2.4 A resolution and its complex structure with inhibitors 3-nitropropionate and 2-thenoyltrifluoroacetone at 3.5 A resolution |
| 1.3.5.1 | hanging drop vapor diffusion method, x-ray structure of mutant E49Q |
| 1.3.5.1 | hanging-drop vapour-diffusion method, the enzyme is cocrystallized with the ubiquinone binding-site inhibitor Atpenin A5 (AA5) to confirm the binding position of the inhibitor and reveal additional structural details of the Q-site |
| 1.3.5.1 | hanging-drop vapour-diffusion, SQR in 20 mM Tris-HCl, pH 7.6, 0.05% THESIT is mixed with an equal volume of reservoir solution containing 100 mM Na-HEPES, pH 7.5, 200 mM, CaCl2 and 28% polyethylene glycol 400, crystals diffract to 2.6 A resolution |
