Crystallization and preliminary X-ray analysis of a peridinin-chlorophyll a protein from Amphidinium carterae.
Crystals of a water-soluble (Mr approximately 39,000) peridinin-chlorophyll a protein from Amphidinium carterae are reported. The crystals diffract to 2.2 A and belong to a monoclinic (B2) and a triclinic (P1) space group. Spectra of the protein in the crystal and in solution are almost identical.
Steck
K
K
Institut für Biophysik und Strahlenbiologie, Universität Freiburg i.Br., FRG.
Wacker
T
T
Welte
W
W
Sharples
F P
FP
Hiller
R G
RG
D000818:Animals; D002338:Carotenoids; D002734:Chlorophyll; D003461:Crystallography; D004141:Dinoflagellida / Q000032:analysis*; D010940:Plant Proteins / Q000648:ultrastructure; D014961:X-Ray Diffraction
D010940:Plant Proteins; D002734:Chlorophyll; C016040:peridinin; D002338:Carotenoids