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Study of macromolecular systems using the wide range of technology platforms available in the Partnership for Structural Biology, including neutron and X-ray diffraction.

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The Life Sciences Group

ILL’s Life Sciences Group is located in the Carl-Ivar Brändén Building (CIBB) and is an integral part of the Partnership for Structural Biology (PSB). The group has direct physical connectivity to ILL and ESRF beamlines that provide advanced capabilities in neutron and x-ray approaches for the study of the structure and dynamics of biological systems using crystallography, solution scattering, and spectroscopic approaches.  The group has routine access to the wide range of technology platforms available within the PSB - which, in addition to the neutron and x-ray scattering facilities, include state-of-the art capabilities in electron microscopy (negative stain and cryo), high field NMR (6 spectrometers from 600 MHz to 950 MHz), AFM, and cell imaging. It also accommodates capabilities for protein/macromolecule production using advanced expression platforms for prokaryotic and eukaryotic expression, and a construct screening platform. For crystallographic work a high throughput crystallisation platform is available, and work on large crystal growth is being developed at both ILL and at IBS. Macromolecular characterisation platforms are also available for mass spectrometry and 1-D NMR, protein sequencing. A well-equipped biophysical platform (dynamic light scattering (DLS), surface plasmon resonance (SPR), circular diochroism (CD), infrared spectroscopy, SEC-MALLS); an analytical ultracentrifugation (AUC) platform is also available.

ILL’s Life Science Group provides advanced capabilities in molecular biology, biochemistry, isotope labelling, and also contains a dedicated Deuteration Laboratory (D-Lab) as a PSB platform for which external user access can be sought through a rapid access peer-review proposal system. The group is also developing a crystallogenesis platform, with a specific focus on the large crystal growth needs of neutron protein crystallography for instruments such as LADI-III (hotlinked to LSS/LADI) and D19 (hotlink to DIFF/D19). Access to these capabilities is available to all scientists of ILL’s member state countries regardless of where the downstream experiments are to be carried out. The Life Sciences Group closely interacts with the ILL instrument groups and plays an active role in supporting staff and PhD students from the LSS, DIFF and Spectroscopy groups involved in biological projects. It also interacts closely with the ESRF Structural Biology Group and its Business Development Office.

 

 

 


Highlights

Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldaseAtomic resolution study of a redox protein: tautomeric shifts, charge transfer and structured hydronium-water-protein networks.Neutron anomalous scattering as a crystallographic  phasing toolDynamics in folded and intrinsically unfolded proteins.Amyloid assembly kinetics in transthyretin using protein deuteration,  mass spectrometry, crystallographyWater dynamics in intact cells of Shewanella oneidensis at high pressureBack exchange phenomena in neutron protein crystallography and characterisation by IR spectroscopy
Ibrahim et al, Scientific Reports 7, 40948Cuypers et al, Angew. Chem. Int. Ed. 52, 1022.Cuypers et al, Scientific Reports 6, 31487Schirò et al, Nature Communications 6, 6490.Yee et al, Angew. Chem. Int. Ed. 55, 9292.Foglia et al, Scientific Reports 6,18862Yee et al, J. Appl. Cryst. 50, 660.