Structural Biology Group
The Structural Biology group operates a world leading suite of synchrotron radiation beamlines dedicated to the study of biological macromolecules. The facility is comprised of three highly intense, tunable beamlines ID14-4, ID23-1 and ID29; two fixed wavelength beamlines ID14-1 and ID14-2; the world's first microfocus beamline dedicated to protein crystallography, ID23-2, and a protein solution scattering beamline ID14-3. The evolution of the facility, in the context of the ESRF upgrade, is encompassed within UPBL10/MASSIF. This facility will have at its core three beam-lines optimised for highly automated, high-throughput sample evaluation.
Research Highlight
The three-dimensional structure of peridinin–chlorophyll-protein (coloured in a rainbow from N- to C- terminal residues) reconstituted with Bacteriochlorophyll-a (red sticks). The structure shows how photons from sunlight are channeled for photosynthesis and that it is performed in the same way by different pigments. See Schulte, T et al. FEBS Lett. 584, 973-978 (2010). Data were collected on beamlines ID23-1 and ID23-2 at the ESRF as well as at the SLS.
X-ray structures of the peridinin–chlorophyll-protein reconstituted with different chlorophylls.
Peridinin–chlorophyll a-protein is a soluble light harvesting antenna which captures the incoming photons using a particular carotenoid called peridinin. In this work, the protein was reconstituted with peridinin using 3 different kind of chlorophylls (Chlorophyll-b, Chlorophyll-d and Bacteriochlorophyll-a). The 3 X-ray crystal structures were solved to resolutions below 2 Å. In all three cases the pigment arrangements are essentially the same as in the native form. Elucidation of the structural properties associated to these 3 variants will help in spectroscopic investigation in order to understand the energy transfer processes which are dominated by the unique properties of the carotenoid peridinin.
Data were collected at beamlines ID23-1, ID23-2 and the SLS
Google map of the ESRF with useful locations
Scientific Output
Research performed at the ESRF produces over 20% of the protein structures submitted in the world and accounts for over 50% of those that come from Europe. To see a list of structures solved at the ESRF see the BIOSYNC website. In order to maintain the predominance of the ESRF in world science, a substantial upgrade programme is in progress; for more information about the upgrade please click here.
Associated Facilities
A number of laboratories and facilities are available to the community. Of particular interest is The Partnership for Structural Biology (PSB) which is a collaboration between ESRF, EMBL, ILL and IBS to bring together a set of complementary technologies for structural biology.