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Crystallization and preliminary X-ray diffraction analysis of the peripheral light-harvesting complex LH2 from Marichromatium purpuratum.

Authors :
Cranston LJ
Roszak AW
Cogdell RJ
Source :
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2014 Jun; Vol. 70 (Pt 6), pp. 808-13. Date of Electronic Publication: 2014 May 24.
Publication Year :
2014

Abstract

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 I4, with unit-cell parameters a=b=109.36, c=80.45 Å. The data appeared to be twinned, producing apparent diffraction symmetry I422. 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.

Details

Language :
English
ISSN :
2053-230X
Volume :
70
Issue :
Pt 6
Database :
MEDLINE
Journal :
Acta crystallographica. Section F, Structural biology communications
Publication Type :
Academic Journal
Accession number :
24915099
Full Text :
https://doi.org/10.1107/S2053230X14009303