Astbury Centre has outstanding expertise and research infrastructure in all of the major techniques in structural biology
The Astbury Centre brings together researchers from across the University - largely from physics, the biological sciences and chemistry - to allow interdisciplinary approaches to be harnessed to understand the molecular basis of life. The Centre has outstanding expertise and research infrastructure in chemical biology, biophysics and all of the major techniques in structural molecular biology. Together, these approaches are combined with analyses of biological function with the ultimate aim of understanding the molecular basis of biological mechanisms in living cells. Our members address major questions associated with biological mechanisms in areas as diverse as membrane proteins; protein folding and assembly; viruses; and motor proteins. The Astbury Centre hosts 4-year PhD programmes funded by the Wellcome Trust and BBSRC that recruit students with the wide range of expertise that may be used to address fundamental biological questions.
Electron microscopy and NMR services are available through Instruct.
Astbury Biostructure Laboratory
Members of the Astbury Centre work in various locations around the campus. The map below shows buildings affiliated with the Astbury Centre. The Astbury Biostructure laboratory electron microscopy facility is based in the Rodger Stephens building (29). The Astbury Biostructure laboratory NMR facility is based in Miall (35).
The Astbury Biostructure Laboratory includes the electron microscopy facility within the Faculty of Biological Sciences. We have a range of state-of-the-art equipment for transmission electron microscopy of biological specimens, from small macromolecular complexes to cells, tissues and organisms.
Our facilities are available to researchers from across the University of Leeds, and external users form academia and industry.
Our facility can operate at Biosafety Level II.
The NMR facility of the Astbury BioStructure Laboratory in Leeds has several unique capabilities available at 950 MHz. The first is based on direct heteronuclear detection (15N and 13C, 5mm TXO Cryoprobe). The combination of high field and Carbon detection has advantages for complex or large intrinsically disordered proteins. There are also new developments in characterising protein sidechains utilising Carbon detection. Techniques using 15N detection are under development and are of interest in chemically exchanging systems, as an alternative to Ca detection and when deuteration is not feasible. The second is based on using a smaller diameter probe (3mm TCI Cryoprobe) for mass limited samples and high ionic strength samples for optimised sensitivity.