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 Death-Associated Protein Kinase (coloured in a rainbow from N- to C- terminal residues) when bound to calmodulin (green, calcium ions magenta). This structure shows how calmodulin is able to activate DAPK kinase by binding to an autoregulatory domain (red). See de Diego et al. Sci. Signal. 3, ra6 (2010). Data were collected on beamlines BM14 and ID29 at the ESRF as well as at DESY.
Molecular Basis of the Death-Associated Protein Kinase–Calcium/Calmodulin Regulator Complex
The large and ubiquitous protein kinases family regulates the majority of cellular pathways and especially those involved in signal transduction. One important subfamily is the calcium/calmodulin (CaM)–dependent protein serine-threonine kinases (CaMKs). An important structural feature of the CaMKs is an extra ‘autoregulatory domain’ (ARD) C-terminal to the catalytic domain. The CaMKs are activated when there is a flood of calcium ions inside the cell that are picked up by the CaM. It has been previously shown that different sites in the ARD are known to be important for the binding of CaM to CaMKs and their subsequent activation. The structure of death-associated protein kinase (DAPK) in complex with CaM shows how the ARD domain facilitates such an interaction. These results provide an important breakthrough in understanding the molecular basis of the more general CaM-CaMKs regulatory system.
Data were collected on the beamlines BM14 and ID29 at the ESRF as well as at DESY.
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.