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Crystallization and preliminary X‐ray diffraction analysis of the peripheral light‐harvesting complex LH2 from Marichromatium purpuratum
Author(s) -
Cranston Laura J.,
Roszak Aleksander W.,
Cogdell Richard J.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14009303
Subject(s) - tetragonal crystal system , crystallography , diffraction , histone octamer , synchrotron radiation , resolution (logic) , crystallization , chemistry , x ray crystallography , materials science , crystal structure , physics , optics , biochemistry , organic chemistry , artificial intelligence , nucleosome , computer science , histone , gene
LH2 from the purple photosynthetic bacterium Marichromatium (formerly known as Chromatium ) purpuratum is an integral membrane pigment–protein complex that is involved in harvesting light energy and transferring it to the LH1–RC `core' complex. The purified LH2 complex was crystallized using the sitting‐drop vapour‐diffusion method at 294 K. The crystals diffracted to a resolution of 6 Å using synchrotron radiation and belonged to the tetragonal space group I 4, with unit‐cell parameters a = b = 109.36, c = 80.45 Å. The data appeared to be twinned, producing apparent diffraction symmetry I 422. The tetragonal symmetry of the unit cell and diffraction for the crystals of the LH2 complex from this species reveal that this complex is an octamer.