Unknown

Dataset Information

0

Seleno-detergent MAD phasing of leukotriene C4 synthase in complex with dodecyl-?-D-selenomaltoside.


ABSTRACT: Dodecyl-?-D-selenomaltoside (SeDDM) is a seleno-detergent with a ?-glycosidic seleno-ether in place of the ether moiety in dodecyl-?-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.

SUBMITTER: Saino H 

PROVIDER: S-EPMC3232166 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Seleno-detergent MAD phasing of leukotriene C4 synthase in complex with dodecyl-β-D-selenomaltoside.

Saino Hiromichi H   Ago Hideo H   Ukita Yoko Y   Miyano Masashi M  

Acta crystallographica. Section F, Structural biology and crystallization communications 20111129 Pt 12


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 crys  ...[more]

Similar Datasets

| S-EPMC4014545 | biostudies-literature
| S-EPMC3931076 | biostudies-literature
| S-EPMC3091245 | biostudies-literature
| S-EPMC5000086 | biostudies-literature
| S-EPMC3003377 | biostudies-literature
| S-EPMC3940196 | biostudies-literature
| S-EPMC44893 | biostudies-other
| S-EPMC3728707 | biostudies-literature
| S-EPMC1218910 | biostudies-other
| S-EPMC5327799 | biostudies-literature