Structural biology

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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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

• ID13
• BM16
• BM26
• BM30A

Locations

Google map of the ESRF with useful locations (click on yellow "pins" for location details)

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).