YSBL maintains its own wet laboratory facilities with the expertise and equipment for gene cloning, PCR, sequencing and protein overexpression in a variety of systems from small to large (fermenter) scales in both bacterial (E. coli) and baculovirus driven insect cell systems. For proterin purification, there are several low and high pressure chromatography systems and a large number of different chromatographic matrices for optimal protein purification. The laboratory has access to a range of biophysical characterisation techniques such as light scattering, a range of mass spectrometers and analytical ultracentrifugation through the Bioscience Technology Facility. This includes access to methods for biomolecular analysis of proteins and their complexes such as UV, fluorescence and time-resolved spectroscopy, microcalorimetry and surface plasmon resonance.
The primary goal of these facilities is to provide a regular supply of pure, homogenous and functional protein for crystallisation.
Please see Chemical Biology Facility.
YSBL maintains a dedicated crystallisation suite, consisting of nanolitre-drop dispensing Mosquito robots, an experimental crystal imaging system and a large, temperature controlled cystallisation room. In addition, there are series of incubators for crystallisation at different temperatures. Staff at YSBL are pioneers in new methods of crystallisation and many of the screens marketed worldwide were invented here.
Please see the X-Ray Facilities.
The Laboratory is the beneficiary of substantial recent investment, amounting to £5m from the Wolfson Foundation, the Wellcome Trust, a Benefactor and the University to augment facilities for Structural Biology and establish cryo-EM in the new Eleanor and Guy Dodson Building (completed 2020). A 200kV electron cryomicroscope (ThermoFisher Glacios) is currently being installed. It is equipped with a field-emission source, Falcon-IV counting direct-electron-detector, and phase-plate, allowing cutting-edge single particle analysis capable of reconstructions beyond 3Å in ideal cases.
The Centre for Magnetic Resonance, located in the Department of Chemistry, includes two instruments equipped for NMR structural studies of protein and of protein:ligand interactions in solution. The Bruker AVANCE 500MHz and Bruker AVANCE II 700MHz spectrometers are both equipped with shielded magnets and triple (1H, 15N, 13C) resonance inverse, broadband inverse and broadband probes.