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.
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Research Highlight
The structure of the sodium-benzylhydantoin transport protein Mhp1. The protein is shown in a lipid bilayer coloured in a rainbow from its N- to C- terminus with transmembrane helices represented by cylinders. See Shimamura et al., Science, 328, 470 – 473 (2010) . The data were collected on ID29.
The structure of the Sodium-Hydantoin Transporter Mhp1 provides insight into an alternating access mechanism for transport
A large family of proteins exist in bacteria that use a concentration gradient (usually of protons) to transport substances into or out of cells against a concentration gradient. Researchers from Imperial College London, Oxford University and the Diamond Light Source Membrane Protein Laboratory have solved the crystal structure of an inward-facing conformation of the sodium-benzylhydantoin transport protein Mhp1 from Microbacterium liquefaciens at 3.8 Å resolution at beamline ID29 at the ESRF. The structure shows the five-helix inverted repeat typical of this family of transporters and complements previously described structures of the outward-facing and occluded states. Comparative analyses of the three structures combined with molecular dynamics simulations allowed a mechanism for the transport cycle in Mhp1 to be proposed. Movement from the outward- to the inward-facing conformations, needed to allow the inward release of sodium and benzylhydantoin, is achieved by a rigid body movement of transmembrane helices 3, 4, 8, and 9 relative to the rest of the protein. Defining the mechanism of these transporters is important as many members of this family allow bacteria to become resistant to antibiotics.
The data were collected on ID29.
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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.