6533b830fe1ef96bd1297952

RESEARCH PRODUCT

Crystallization of Light-Harvesting Complex II From Vicia Faba (Fabaceae)

K. HartmannR. NickelAloysius Wild

subject

Electron crystallographyChemistryFabaceaelaw.inventionVicia fabachemistry.chemical_compoundCrystallographylawChlorophyllThylakoidBotanyChlorophyll bindingCrystallizationLight harvesting complex II

description

The most abundant chlorophyll binding complex in plants is the intrinsic light-harvesting complex II (LHC II), comprising about half of the total chlorophyll in thylakoid membranes. The structure of LHC II has been determined by electron crystallography, providing a three-dimensional map at 3.4 A (1). Nevertheless, high-resolution structure based on x-ray crystallography is still missing because of the lack of highly ordered 3-D crystals. While delipidation of membrane proteins suitable for high-quality 3-D crystals seems to be a prerequisite, in case of LHC H delipidation leads to a loss of the ability to crystallize. So far, standard purification methods like chromatography have been proofed not to be suitable for purification of LHC H from pea, according to a monomerization of the complex by intensive delipidation. We have investigated the possibility to get highly ordered 2-D as well as 3-D crystals from broad bean (Vicia faba) LHC II purified by ionexchange chromatography.

yearjournalcountryeditionlanguage
1998-01-01
https://doi.org/10.1007/978-94-011-3953-3_84