Structural biology
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The Structural Biology group operates a world leading suite of synchrotron radiation beamlines dedicated to the study of biological macromolecules:
Snapshots of all beamlines are available through the Find a Beamline page.
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Current Research Highlight
The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre. Hydrogenases catalyse the conversion of H2 into protons and electrons and are often oxygen intolerant. A new structure of an oxygen tolerant hydrogenases reveals the mechanism of hydrogenase oxygen tolerance. See Fritsch et al., Nature, 479, 249-252 (2011).
Hydrogenases are enzymes responsible for the conversion of H2 into protons and electrons and are considered a central constituent in the creation of enzymatic fuel cells and light driven H2 production. Many hydrogenases do not maintain their activity in the presence of oxygen, which severely limits their industrial potential. While certain hydrogenases are O2 tolerant it is still unclear how they protect their active site from the gas. Fritsch et al. report the crystal structure of an O2 tolerant hydrogenase. The catalytic site is connected to three different iron-sulphur clusters responsible for the electron transport from the active site into cytochrome b. Proximal to the active site is a 4Fe-3S structure coordinated by six cysteins. This iron sulphur cluster is able to adopt three redox states under physiological conditions and is proposed to act as a switch which serves as an electron acceptor upon H2 oxidation, but also protects the active site by serving as an electron donor, which upon O2 attack delivers the necessary electrons required for the complete reduction of O2 to water, freeing the active site. These results have implications for the rational design of more efficient O2 tolerant Hydrogenases
Data were collected at ESRF beamline ID14-4 and BESSY II
Introducing structural biology at the ESRF
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The evolution of the facility, in the context of the ESRF upgrade, is encompassed within UPBL10/MASSIF. This facility, to be located at beamlines ID30 and BM29, will have at its core three beamlines optimised for highly automated, high-throughput sample evaluation. |
Industrial applications
Many of the world's leading pharmaceutical companies carry out proprietary research on our beamlines developing future drug candidates. Industrial clients can access our facilities through our mail-in crystallography service MXpress or by applying directly for beamtime. See the Industry website for details.
In-house research
In-house research runs in parallel to beamline operation, helping us to perfect techniques while investigating key scientific areas. Current projects include:
- Beamline instrumentation (Kappa gonimeters, dehydration devices, sample characterisation)
- The molecular basis of the extreme radiation resistance of Deinococcus radiodurans
- Structural studies of enzymatic transition states
- Activation mechanisms of LysR transcription regulators.
Additional details are in our Research & Development and Research Profiles pages.
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.
- The Partnership for Structural Biology
- Cryo-Bench Laboratory
- BM14 - ESRF beamline managed and operated by a
consortium between EMBL and NII, India, permitting European and
Indian access. Both public (ESRF) and consortium beamtime (40 and
60%, respectively) are offered.
Collaborating Research Group beamlines
Locations
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Google map of the ESRF |
Research highlights
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. The following are some recent results (view highlights listing).
How GPCRs get their message accross
G protein-coupled receptors (GPCRs) are enormously important drug targets, accounting for about 30% of approved drugs with many hundreds of drugs currently in development also targeting them. New structures reveal how they respond to their signalling molcules… (22-11-2011)
A Dual Binding Mode for RhoGTPases in Plexin Signalling
Plexins are a type of cell surface receptor that have been implicated in oncogenesis. New structures of Plexin B1 have allowed a model of signalling to be proposed.… (03-11-2011)
Snapshot of a bacterial transporter in the act of secreting a protein
ID29 - protein crystallography (Spotlight, 04/10/2011)…



