6533b860fe1ef96bd12c3a9d
RESEARCH PRODUCT
Crystallization and preliminary X-ray studies of oligandrin, a sterol-carrier elicitor fromPythium oligandrum
Michel PonchetMarie-bernard LascombeJean-pierre BleinFranck PanabièresThierry PrangéMarie-louise Milatsubject
Protein ConformationPythiumElicitinGeneral MedicineBiologyCrystallography X-Raybiology.organism_classificationSterolElicitorlaw.inventionFungal ProteinsSterolsCrystallographyCholesterolSterol carrier proteinStructural BiologylawPEG ratioIntercellular Signaling Peptides and ProteinsMoleculeElectrophoresis Polyacrylamide GelCrystallizationCarrier ProteinsCrystallizationPythium oligandrumdescription
Oligandrin is a 10 kDa acidic protein produced by the fungus micromycete Pythium oligandrum and is a member of the alpha-elicitin group, with sterol- and lipid-carrier properties. Oligandrin has been crystallized at 290 K using PEG 4000 as a precipitant. A cholesterol complex was obtained under the same conditions. The space group of the crystals at low temperature (100 K) is C222, with unit-cell parameters a = 94.0, b = 171.1, c = 55.3 A. Four molecules are present in the asymmetric unit. Data from the free and cholesterol-complexed forms were recorded at synchrotron sources to resolutions of 2.4 (uncomplexed) and 1.9 A (complexed), respectively.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2000-06-16 | Acta Crystallographica Section D Biological Crystallography |