The Structural Biology group operates a world leading suite of synchrotron radiation beamlines dedicated to the study of biological macromolecules:
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.
FAM3B PANDER and FAM3C ILEI Represent a Distinct Class of Signaling Molecules with a Non-Cytokine-like Fold, Johansson, P., Bernström, J., Gorman, T., Öster, L., Bäckström, S., Schweikart, F., Xu, B., Xue, Y. & Holmberg Schiavone, L., Structure 21, 306-313 (2013); DOI: 10.1016/j.str.2012.12.009.
Orthogonal views of the crystal structure of FAM3B PANDER showing its novel β-β-α fold.
Summary: The structures of two members of the FAM3 superfamily - FAM3B PANDER, implicated in the regulation of glucose homeostasis and β cell function; FAM3C ILEI, implicated in epithelial-mesenchymal transition and cancer - were predicted to be very similar to the four-helix bundle fold seen for other cytokines. However, the crystal structure of FAM3B PANDER shows that, unexpectedly, this protein adopts a novel β-β-α fold, similar only to that of the theoretical, ab initio-designed protein TOP7. This novel fold is conserved for the entire superfamily and it is thus very likely that FAM3 members represent a new structural class of signalling molecule with a different mode of action compared to that observed for the well-known four-helix bundle group of cytokines. The crystal structure of FAM3B PANDER was determined by the S-SAD technique using diffraction data collected at l = 2.06 Å (E = 6.0 keV) from a single crystal, space group P212121. Although anomalous signal was observable only to relatively low (dmin = 4.5 Å) resolution in the processed data set, a sulphur atom substructure representing disulphide bridges was determined using direct methods and split into separate atoms. Iterative refinement of the S atom positions was then carried out using density modification Hendrickson Lattman coefficients as phase restraints before a final round of statistical density modification and phase-extension to dmin - 2.3 Å.
Data collected on ID29.
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.
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 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.
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