ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Seleno-detergent MAD phasing of leukotriene C4 synthase in complex with dodecyl-β-D-selenomaltoside.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Heavy Atom Detergent/Lipid Combined X-ray Crystallography for Elucidating the Structure-Function Relationships of Membrane Proteins.Membranes · 2021Review
- Sweet Selenium: Synthesis and Properties of Selenium-Containing Sugars and Derivatives.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Membrane protein structure determination by SAD, SIR, or SIRAS phasing in serial femtosecond crystallography using an iododetergent.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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4 authors.
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Abstract
Dodecyl-β-D-selenomaltoside (SeDDM) is a seleno-detergent with a β-glycosidic seleno-ether in place of the ether moiety in dodecyl-β-D-maltoside. Seleno-detergents are candidates for heavy-atom agents in experimental phasing of membrane proteins in protein crystallography. Crystals of a nuclear membrane-embedded enzyme, leukotriene C(4) synthase (LTC(4)S), in complex with SeDDM were prepared and a multiwavelength anomalous diffraction (MAD) experiment was performed. The SeDDM in the LTC(4)S crystal exhibited sufficient anomalous diffraction for determination of the structure using MAD phasing.
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