Gothenburg researchers make world top ten

A professor of biochemistry, Richard Neutze, and research colleagues Gergely Katona, Linda Johansson and David Arnlund, are part of an international collaboration developing new approaches to structural biology using X-ray lasers. This collaboration also includes groups from Germany and the USA.

“It’s a big deal for representatives of the University of Gothenburg to co-author an article that is ranked as a Scientific Highlight by the journal Science,” says Richard Neutze.

International collaboration

The article highlighted by Science is part of a long-term international research collaboration which has developed new ways of using extremely short and intense X-ray pulses generated by an X-ray laser to determine a protein’s structure at molecular level. This approach combines diffraction data from thousands of nanocrystals that are too small to be seen using a normal microscope.

“Our collaboration has published several articles in Nature, Science and Nature Methods during the last two years that lay the foundations for this new approach to structural biology,” says Richard Neutze.

Hope for new treatments

The article selected as a scientific highlight for 2010 by Science presents the first new protein structure using an X-ray laser, and may help to identify new medicines for trypanosomiasis, also known as sleeping sickness or African lethargy. More than 60 million people a year are infected with sleeping sickness, and around 30,000 die as a result. Caused by the Trypanosoma brucei parasite, the disease is carried by tsetse flies and infects the blood and lymph system before invading the brain.

One of the proteins in the parasite is a promising starting point for developing new treatments for sleeping sickness. But until now it has not been possible to obtain sufficient information on the structure of the protein to develop a safe and specific medicine. Using very short (femtosecond) X-ray pulses the research group has now obtained information about the molecular structure of this protein with a natural inhibitor bound to it, potentially aiding the identification of new medicines for sleeping sickness.