The Synchrotron Crystallography Team works in close collaboration with the Structural Biology Group of the European Synchrotron Radiation Facility (ESRF) in the design, construction and operation of macromolecular crystallography (MX) and biological small angle X-ray scattering (bioSAXS) beamlines. We are currently co-responsible for the microfocus MX beamline on ID23-2, the fully automatic MX beamline on MASSIF-1/ID30A-1, the tunable MX beamline on ID30B and the new serial MX (SMX) beamline on ID29. We’re also developing a web based graphical user interface, BSXCuBE3, for the bioSAXS beamline at BM29. Further information on these facilities can be found on the EMBL Grenoble services webpage. In addition, we work in close collaboration with the Papp team on the design and user aspects of new scientific instruments. We also actively contribute in the design and implementation of complex MX and bioSAXS experimental workflows for automated sample screening, data collection and analyses.
In the laboratory, we study proteins involved in neuronal development, particularly the Slit-Robo signalling complex; Autotaxin ─ an important lysophospholipase implicated in many pathological diseases; RNA writer proteins in collaboration with the Pillai group at the University of Geneva, phosphoryl transfer proteins, and proteins involved in the Toxoplasma gondii immune evasion in collaboration with Dr. Hakimi of Grenoble Medical University.
The ESRF Extremely Brilliant Source began user operation in August 2020. Significant instrument and software upgrades were completed on all ESRF-EMBL Joint Structural Biology Group Beamlines while MASSIF-1 and BM29 underwent major refurbishments in 2020. On MASSIF-1 a new MD2S diffractometer and FlexHCD sample changer were installed for increased sample throughput and a CrystalDirectTM harvester was installed to allow direct sample delivery from crystallisation plates. On BM29 we’re leading the development of BSXCuBE3. The new SMX beamline on ID29 opened to user in October 2022 and the commissioning of new SMX experiments are underway. To harness the unique scientific potential of the fourth generation ESRF-EBS X-ray beams for European structural biologists we will continue to develop web based user interfaces and more sophisticated automated data collection and analyses methods. We hope all these combined efforts will have an impact on future challenging structural biology projects.
In the laboratory, we will continue our research on the Slit-Robo signalling complex by trying to decipher how exactly Slit activates Robo on the cell surface. We will also continue our studies on the mechanistic selection and activation of MAP (mitogen-activated protein) kinases by upstream MAPK kinases as well as their subversion by T. gondii. Lastly, we will continue our work on Autotaxin and RNA writers.