Dataset Information


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.


PROVIDER: S-EPMC2531281 | BioStudies | 2008-01-01

REPOSITORIES: biostudies

Similar Datasets

1979-01-01 | S-EPMC1186413 | BioStudies
2020-01-01 | S-EPMC7302508 | BioStudies
1978-01-01 | S-EPMC1186051 | BioStudies
2012-01-01 | S-EPMC3418823 | BioStudies
2017-01-01 | S-EPMC5174144 | BioStudies
2016-01-01 | S-EPMC5148649 | BioStudies
2009-01-01 | S-EPMC2790596 | BioStudies
1000-01-01 | S-EPMC2877156 | BioStudies
2013-01-01 | S-EPMC3736684 | BioStudies
2021-01-01 | S-EPMC7792994 | BioStudies