SPIE member Henry Chapman, a scientist from the Deutsches Elektronen-Synchrotron (DESY) lab in Germany, has been awarded the Leibniz Prize for his pioneering work in the development of femtosecond crystallography.
Sponsored by the German research foundation Deutsche Forschungsgemeinschaft (DFG), the €2.5 million prize was announced on 10 December.
Until now, decoding biomolecules out of the natural environment has been complex and nearly impossible. Chapman's new method for collecting crystallographic information decodes the structure of complex biomolecule crystals at the atomic level, with the help of X-ray lasers. When the biomolecule crystals are illuminated by the X-ray light they are forced out of their environment and reflect a scattering image of their structure.
Chapman participated in studies conducted at the SLAC National Accelerator Laboratory's two mile long linear accelerator or the Linac Coherent Light Source (LCLS).
Femtosecond crystallography has been used to create medication against sleeping sickness. As the leading scientists at DESY, Chapman decoded the structure of the Cathepsin B enzyme, which is key to the survival of the sleeping sickness parasite responsible for African trypanosomiasis.
Chapman's SPIE profile
SLAC press release