Frank has been head of the PX group since the start of the SGC in 2004, focussing on methodology and high-throughput techniques for protein crystallography. In late 2012 he joined the Diamond Light Source synchrotron as head of beamline I04-1. In this role he is working to make Fragment Screening by X-ray Crystallography an easily accessible and routine experiment for both academic and industrial users.
Frank received his undergraduate degree from the University of the Free State (Bloemfontein, South Africa), and gained his PhD in protein crystallography under Tom Blundell at Cambridge (UK). He has also worked as a postdoc in San Diego (academically at Scripps in the JCSG, industrially at Syrrx in its pre-Takeda days). He is a visiting professor at the Biochemistry Department of the University of Johannesburg.
The context of our research is the SGC pursuit of structures and chemical probes. Our group collaborates closely within the whole SGC, enabling massively parallel crystallization of all purified proteins using our general-access infrastructure, and ensuring that crystals are solved by in-house testing, synchrotron data collection and rapid structure solution – an ideal environment for methods development. Our scientific focus is how crystallography can truly transform cost and efficiency in protein-targeted chemistry – possible in principle, but difficult to achieve in practice. We thus address the methodology of: (1) ease-of-use and accessibility for all steps in crystallography, from crystallization to structure solution; and hence, (2) how to generate ligand-bound structures reliably and rapidly, to allow crystallography to become a truly routine assay for ligand binding. The PX group offers opportunities both in structure projects, to gain extensive experience rapidly; and in developing methodologies, including: characterization of protein quality; calculating protein crystallizability; crystal optimization; non-manual harvesting of crystals; serial optimized data collection; massively parallelized structure solution; ligand solubility and crystal soaking protocols.