Using a unique facility in the US, researchers at the University of Gothenburg have found a more effective way of imaging proteins. The next step is to film how proteins work at molecular level.
Mapping the structure of proteins and the work they do in cells could be the key to cures for everything from cancer to malaria. Last year Richard Neutze, professor of biochemistry at the University of Gothenburg, and his research group were among the first in the world to image proteins using very short and intensive X-ray pulses.
In a new study published in Nature Methods, the method has been tested on a new type of protein, with good results.
"To put it simply, we've developed a new method of creating incredibly small protein crystals," says Linda Johansson, doctoral student at the Department of Chemistry and Molecular Biology and lead author of the article. "We've also shown that it's possible to use very small crystals to determine a membrane protein structure."
Could become standard
There are two major challenges when it comes to imaging proteins: the first is to create the right sized protein crystals, and the second is to irradiate them in such a way that they do not disintegrate. Although Sweden has a facility for synchrotron-generated X-ray radiation Maxlab in Lund this type of technology is not sufficiently light-intensive and therefore requires large protein crystals which take several years to produce.
Richard Neutze was one of the researchers to float the idea that it might be possible to image small protein samples using free-electron lasers which emit intensive X-ray radiation in extremely short pulses shorter than the time it takes light to travel the width of a human hair. This kind of facility has been available in California since 2009, and it is this facility that was used for the study.
"Producing small protein crystals is easier and takes less time, so this method is muc
|Contact: Linda Johansson|
University of Gothenburg