title: Screening of detergents for solubilization, purification and crystallization of membrane proteins: a case study on succinate:ubiquinone oxidoreductase from Escherichia coli.
abstract: Succinate:ubiquinone oxidoreductase (SQR) was solubilized and purified from Escherichia coli inner membranes using several different detergents. The number of phospholipid molecules bound to the SQR molecule varied greatly depending on the detergent combination that was used for the solubilization and purification. Crystallization conditions were screened for SQR that had been solubilized and purified using 2.5%(w/v) sucrose monolaurate and 0.5%(w/v) Lubrol PX, respectively, and two different crystal forms were obtained in the presence of detergent mixtures composed of n-alkyl-oligoethylene glycol monoether and n-alkyl-maltoside. Crystallization took place before detergent phase separation occurred and the type of detergent mixture affected the crystal form.
authors.affiliation: Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
authors.forename: Hironari
authors.initials: H
authors.lastname: Shimizu
authors.forename: Coh-ichi
authors.initials: C
authors.lastname: Nihei
authors.forename: Daniel Ken
authors.initials: DK
authors.lastname: Inaoka
authors.forename: Tatushi
authors.initials: T
authors.lastname: Mogi
authors.forename: Kiyoshi
authors.initials: K
authors.lastname: Kita
authors.forename: Shigeharu
authors.initials: S
authors.lastname: Harada