Macromolecular crystallography is a technique used to determine the atomic structure of biological macromolecules, such as proteins and nucleic acids.
It works by using crystals (grown by purifying the protein or nucleic acid under the right conditions) and exposing them to X-ray beams. As the X-rays pass through the crystal, they are diffracted in various directions, creating a unique pattern. This diffraction pattern is captured by a detector, providing information about the electrons within the crystal.
The specialised software at Diamond processes the diffraction data to create a 3D electron density map. This map shows where the electrons are located within the crystal. Researchers then use the electron density map to build a model of the macromolecule, showing the arrangement of atoms.