The outstanding success of structural biology within the last two decades is closely related to the development and evolution of macromolecular crystallography (MX) beamlines. Indeed, many of today's synchrotron-based MX experimental sessions aim for fast but rigorous evaluations and data collections from very large numbers of samples [1–7]. To facilitate this, sample changing on most MX beamlines is now carried out by robots and the centering of a crystal in the X-ray beam to micrometer precision is now automatically performed using either optical or diffraction-based techniques . Once a crystal is centered, users have a wide array of options at their disposal to prepare any given experiment. This includes: X-ray fluorescence (XRF)  analysis to confirm the presence of anomalous scatterers in crystals; X-ray absorption near-edge scans (XANES) to determine the best X-ray wavelengths for MAD/SAD data collection ; and the probing of the diffraction properties of crystals to determine the best crystal, or area of a crystal , for data collection. All of these operations are now also automated, as is the collection of the final diffraction data set either from single or multiple crystals and the subsequent data analysis and reduction.
- Acceleratorfysik och instrumentering