The behaviour and function of proteins is largely determined by their shape. So one of the great ongoing quests in biology is to understand and model the structure of proteins.
That's a tricky task. Biologists currently do it using techniques such as X-ray crystallography, which requires millions of protein chains to form into a crystal. The trouble is that most proteins don't form crystals. And even when they do, not all the molecules will be in the same conformation and so the diffraction pattern can end up being a kind of average of several different shapes.
That's why biologists know the shape of less than 2 per cent of the proteins in humans.
What's needed, of course, is a way of imaging individual proteins. One idea is to us x-rays or electron beams to do the trick and indeed some groups have had some success with this technique. But the disadvantage is that beams with an energy of a few KeV tend to destroy biomolecules so it's not clear how accurate these images can be. Nether is it possible to view the molecules over time.
Today, Jean Nicholas Longchamp and pals at the University of Zurich in Switzerland have found a way round this. These guys make the entirely sensible suggestion of imaging proteins using low energy electron beams that don't destroy biomolecules.
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