ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Screening of detergents for solubilization, purification and crystallization of membrane proteins: a case study on succinate:ubiquinone oxidoreductase from Escherichia coli.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 2 citations in OpenAlex.
- Fluorescence-Detection Size-Exclusion Chromatography-Based Thermostability Assay for Membrane Proteins.Methods in molecular biology (Clifton, N.J.) · 2023Article
- An improved fluorescent tag and its nanobodies for membrane protein expression, stability assay, and purification.Communications biology · 2020Article
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6 authors at 2 institutions in 1 country.
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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.
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