There is often a competition, explicit or implied, between NMR spectrometrists and X-ray crystallographers. A new technique merges the best of both worlds
Researchers at the University of Shutka, Russia, have constructed a unique NMR spectrometer with a hole bored all the way through the magnet and probe, perpendicular to the main sample cavity. This hole allows the researchers to send an X-ray beam directly into a crystal mounted in a specially designed sample chamber, allowing them to screen for compound binding by NMR while simultaneously obtaining crystal structures. Of course, due to the solid state (crystalline) form of the protein, the researchers can’t actually detect the protein itself by NMR, but by mounting the crystal in a flow cell and testing pools of fragments, they can use target-based NMR to determine which fragments bind to the protein. Once they find a fragment that binds, they can then immediately obtain the crystal structure. The researchers are planning to bring their NMR to a synchrotron to have access to a brighter X-ray source.
Will the technique become widely accepted? If so, this could be the start of a beautiful friendship.