Until now, the primary way to obtain a high-resolution model of a protein’s structure was through a method called X-ray crystallography. In this technique, a solution of proteins is turned into a crystal, itself a difficult and time-consuming process, and then this crystal is bombarded with X-rays, often from a large circular particle accelerator called a synchrotron. The diffraction pattern of the X-rays allows researchers to build up a picture of the internal structure of the protein. It takes about a year and costs about $120,000 to obtain the structure of a single protein through X-ray crystallography, according to an estimate from the University of Toronto. More recently, two other experimental methods—nuclear magnetic resonance and cryogenic electron microscopy—have also been used. They can be faster and less expensive but tend to produce models that are less precise than X-ray crystallography.