Cornelius Gati. Photograph: Private

The Association of the Friends and Supporters of DESY (VFFD) has awarded its 2016 prize for doctoral students to Cornelius Gati.

The VFFD is doing so in recognition of Gati’s doctoral thesis entitled “Data processing and analysis in serial crystallography at advanced X-ray sources”, which was researched at DESY and the University of Hamburg, and which was financed with a Helmholtz scholarship of the PIER Helmholtz Graduate School. The award was presented on the occasion of the DESY Science Day on 2 December 2016 in the main auditorium.

Gati, who was born in Kirchheim unter Teck in 1987, studied biology at the Eberhard Karls University in Tübingen and was awarded a Bachelor of Science in Biology in 2010. After attending the Technical University in Munich and working at Roche Diagnostics GmbH, he was awarded his Master of Science in 2012 by the Paul Scherrer Institute in Switzerland. He then started working on his PhD at DESY at the Center for Free-Electron Laser Science, CFEL, looking at methods of investigation using X-ray lasers.

X-ray free-electron lasers allow experiments to be carried out with a higher temporal resolution than ever before. They can capture the image of a biomolecule so quickly that the image is not affected by any damage done to the molecule’s structure. In his dissertation, Gati describes various examples of how the technique can be applied, such as the hitherto smallest protein crystals for which data has ever been collected on an atomic scale, the first structure of a human membrane protein at room temperature, and the first completely unknown protein structure to be solved using serial femtosecond crystallography (SFX). In the latter case, important insights were obtained about a receptor that is of huge pharmacological significance and plays a key role in high blood pressure.

Another part of Gati’s dissertation describes in detail how the SFX technique can be adapted to a modern microfocus measuring station using a conventional source of synchrotron radiation. The main advantage of this synchrotron-based method is the possibility of giving a wide range of structural biologists the opportunity of examining small protein crystals, just a few micrometres across, both at cryogenic and at room temperatures.

Currently, Gati works as postdoctoral researcher at the Laboratory of Molecular Biology (LMB) - Medical Research Council (MRC), Cambridge, UK.


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