One of the great challenges in molecular biology is to determine the three-dimensional structure of large biomolecules such as proteins. But this is a famously difficult and time-consuming task.
The standard technique is x-ray crystallography, which involves analyzing the x-ray diffraction pattern from a crystal of the molecule under investigation. That works well for molecules that form crystals easily.
But many proteins, perhaps most, do not form crystals easily. And even when they do, they often take on unnatural configurations that do not resemble their natural shape.
I love cryo-electron microscopy. It could only work in a computer age when hardware can overlay thousands of molecules seen in the EM to reconstruct a 3D image.
It works especially well with really large proteins, something hard to do with X-ray crystallography. Now we can do it 100,000 faster.
Image: Peer J