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

DOI: 10.1107/S2053230X14009303 DOI Help
PMID: 24915099 PMID Help

Authors: Laura J. Cranston (University of Glasgow) , Aleksander Roszak (University of Glasgow) , Richard J. Cogdell (University of Glasgow)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 , PAGES 808 - 813

State: Published (Approved)
Published: June 2014
Diamond Proposal Number(s): 6683

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 A ° using synchrotron radiation and belonged to the tetragonal space group I4, with unit-cell parameters a = b = 109.36, c = 80.45 A ° . 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.

Subject Areas: Biology and Bio-materials, Energy

Instruments: I02-Macromolecular Crystallography

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