Few fields of research have benefitted as significantly as structural biology from interdisciplinary synergies between lab-bench scale science on the one hand and large scale research infrastructure on the other. For almost four decades synchrotron radiation physicists, beamline engineers and protein crystallographers have cooperated to drive the field forwards.
The outcome has been a spectacular growth in the rate at which new protein structures are solved. The scientific output of this endeavour is illustrated by six Nobel Prizes in Chemistry (Michel, Deisenhofer, Huber 1988; Walker 1997; McKinnon 2003; Kornberg 2006; Steitz, Yonath, Ramakrishnan 2009, Kobilka 2012), whose breakthroughs derive from diffraction data collected using synchrotron radiation. It is of crucial relevance to underline that the use of synchrotron radiation for structure-based drug design has become mainstream within pharmaceutical industry.
Very close cooperation between traditionally separate fields of research continues to be absolutely essential at the very cutting edge of structural biology. These opportunities include the use of short-pulsed X-ray sources for extracting time-dependent structural information from proteins; and the revolutionary new possibilities created by X-ray Free Electron Lasers, which combine ultrafast X-ray pulses with high brilliance focussing capabilities to create an entirely new regime of pre-damage time-resolved serial femtosecond crystallography on unprecedented time-scales.
Exploitation of the new scientific opportunities created by the changing technical landscape requires close interdisciplinary collaboration between structural biologists, physical chemists, beamline engineers, software developers, and industrial partners.