Structural biology

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.

Featured Highlight

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 (d_min = 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.

Link: http://www.cell.com/structure/abstract/S0969-2126%2812%2900464-9

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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)

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