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Literature summary for 1.3.5.1 extracted from

  • Shimizu, H.; Nihei, C.; Inaoka, D.K.; Mogi, T.; Kita, K.; Harada, S.
    Screening of detergents for solubilization, purification and crystallization of membrane proteins: a case study on succinate:ubiquinone oxidoreductase from Escherichia coli (2008), Acta Crystallogr. Sect. F, 64, 858-862.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli K12 strain Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
inner membrane succinate-quinone oxidoreductase is solubilized and purified from Escherichia coli inner membranes Escherichia coli
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Purification (Commentary)

Purification (Comment) Organism
succinate-quinone oxidoreductase is solubilized and purified using detergents 2.5% (w/v) sucrose monolaurate and 0.5% (w/v) Lubrol PX Escherichia coli

Synonyms

Synonyms Comment Organism
SQR
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Escherichia coli
succinate:ubiquinone oxidoreductase
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Escherichia coli