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The PX-SRF manages a state-of-the art crystallography facility optimized for high-throughput and non-expert crystallization and structure solution. As such the experimental facilities and workflows can be used by CMD staff, visiting scientists and collaborators with minimal training required. In addition, our standard practice for crystallography aligns with the best practice for XChem fragment screening, ideally positioning us as feeder facility for XChem experiments.

Our 3 focus areas

Walk-in facilities:

The walk-in facility directly supports 12 CMD PIs and is routinely used by 25 CMD scientists; it also hosts researchers from Oxford departments and external academic collaborators. The facility currently encompasses all devices and consumables required for conducting high throughput protein crystallography experiments and handles all the administrative and reporting tasks involved in samples to the Diamond Light Source for measurement and XChem fragment screening through the block allocation group (BAG) allowances to the CMD.

Crystallography & Ligands:

We support and design protein crystallography experiments tailored to early stage SBDD projects, encompassing all relevant experimental steps: expression construct design and engineering, protein purification, crystallization, structure determination and analysis, preparation of protein-ligand structures and small molecule compound design.  Project planning and grant writing are also supported.  These services are offered to all internal and external scientist on a collaborative basis, including industrial partners.

Technology advancement:

This focus area includes both early development of leading-edge technologies and approaches, and crucially deployment into definable platforms, that add value and credibility to users’ funding proposals, and transformative efficiency to their funded science.  (Exemplars are the ASAP and PROTECT awards.)

The current developments and platforms comprise:  PREPX (in use) for the parallelised protein purification and crystallization; low-cost bag-based expression for larges volume or extensively varied protein production; engineering crystallization with Gluebodies or Crysalins mediators; and generating chaperones by ribosome display.