Screening of detergents for solubilization, purification and crystallization of membrane proteins: a case study on succinate:ubiquinone oxidoreductase from Escherichia coli

摘要

Succinate:ubiquinone oxidoreductase was solubilized and purified from E. coli inner membranes using several different detergents and the phospholipid content of each preparation was analyzed. The preparation with the lowest phospholipid content crystallized in two different crystal forms using detergent mixtures composed of n-alkyl-oligoethylene glycol monoether and n-alkyl-maltoside.