https://phys.org/news/2018-05-high-precision-instrument-enables-rapid-protein.html

For this technique to work, proteins must be crystallized—and the most challenging proteins often only grow into tiny microcrystals. To reconstruct these complex protein structures, scientists need to measure X-ray diffraction data from thousands of microcrystals and merge the collected data, a technique called serial crystallography. These measurements currently take hours at highly specialized and advanced research instruments at synchrotron macromolecular crystallography beamlines to complete. Macromolecular crystallography beamlines can be found at nearly every synchrotron radiation facility in the world and use the light sources' intense x-rays to characterize the proteins' atomic structure.

"Using our new ultra-high speed and high-precision FastForward MX goniometer, we are able to collect serial crystallography data so fast that complete datasets can now be acquired in just a few minutes," said Martin Fuchs, the lead scientist at the Frontier Microfocusing Macromolecular Crystallography (FMX) beamline at NSLS-II. "Our new goniometer takes full advantage of the exceptional beam properties of NSLS-II, and therefore of the world-leading bright x-rays available at our beamline."