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

Cranston, L. J., Roszak, A. W. and Cogdell, R. J. (2014) Crystallization and preliminary X-ray diffraction analysis of the peripheral light-harvesting complex LH2 from Marichromatium purpuratum. Acta Crystallographica. Section F: Structural Biology Communications, 70(6), pp. 808-813. (doi:10.1107/S2053230X14009303)

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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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Cogdell, Professor Richard and Roszak, Dr Aleksander
Authors: Cranston, L. J., Roszak, A. W., and Cogdell, R. J.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
College of Science and Engineering > School of Chemistry
Journal Name:Acta Crystallographica. Section F: Structural Biology Communications
Publisher:Wiley-Blackwell Publishing, Inc.
ISSN:1744-3091
ISSN (Online):1744-3091

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