DESY scientist Professor Henry Chapman will be awarded one of the prestigious Gottfried Wilhelm Leibniz Prizes 2015 by the German research foundation Deutsche Forschungsgemeinschaft (DFG), the DFG announced on Wednesday in Bonn. This important research award in Germany honours outstanding scientists. Henry Chapman receives the 2.5-Million-Euro prize for his pioneering work in the development of femtosecond crystallography. It allows to decode the structure of complex biomolecules in its natural environment at the atomic level with the help of X-ray lasers.

“I cordially congratulate Henry Chapman on winning of this prestigious prize. He designed and lead to application the method of serial femtosecond crystallography which for the first time allows to investigate the atomic structure of biological samples in an almost natural environment,” said Professor Helmut Dosch, Chairman of the DESY Board of Directors. “Chapman’s pioneering work in this field will facilitate the analysis of molecular dynamics of highly complex systems. This will revolutionise biological structure research on a global scale and significantly influence its agenda in the coming decades.”

The atomic structure of biomolecules has an elementary influence on its function in the biological system. That is why scientists try very hard to decode these structures, e.g. to find approaches to produce new medication. In this connection crystallography plays a central role: when crystals are irradiated with X-ray light, they scatter the X-rays in a characteristic way. The resulting scattering image allows to calculate the structure of the building blocks of the crystal – in the case of a biomolecule crystal, this is the structure of its molecules.

Frequently, this structure analysis is carried out with the intensive X-ray light of large-scale synchrotron radiation sources such as PETRA III at DESY. Up until now, it has been possible to decode the structure of about 85 000 proteins. However, when using conventional synchrotron radiation sources, it is necessary to combine molecules to regular crystals in order to obtain a sufficiently intensive scattering image for structure calculation. This process is often very complex, sometimes impossible; moreover, the crystallisation rips the biomolecule out of its natural environment.

Novel free-electron X-ray lasers like the European XFEL, currently under construction in Hamburg, produce unprecedentedly brilliant and short X-ray flashes. Its light flashes with a length of only about some millionths of a billionth of a second will be more brilliant than today’s light sources. This opens up the possibility to scientists to decode the atomic structure of complex molecules with tiny nanocrystals, presumably completely without crystallisation in the future. These crystals with the size of only billionths or millionths of a metre are much easier to produce than their larger species. In serial femtosecond crystallography, a beam of these tiny crystals is traversed by X-ray laser light and hundreds of thousands scattering images are taken. The series of single X-ray laser images allows to calculate the overall structure.

Chapman, leading scientist at DESY, is the pioneer in the development of this investigation method especially tailored for free-electron lasers. Using the method, he dissolved the structure of the Cathepsin B enzyme, which is a promising starting point to create a medication against sleeping sickness. The scientific journal “Science” listed his work among the ten most important discoveries in the year 2012. Chapman’s finding of rescuing the scattering image with X-ray lasers before destruction by the intensive light also creates the preconditions to investigate samples almost in their natural environment, thus providing verifiable information about the structure and function of about 100 000 biomolecules which have not yet been decoded.

 

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