The performance of integrated home-lab X-ray systems for protein crystallography has increased substantially in the last decade. Improvements in source technology like the IµS-DIAMOND or the ultra-bright METALJET have made data collections faster. Large area photon-counting detectors such as the PHOTON III [1] are now affordable options for the home-lab and allow accurate data to be collected from very small, poorly diffracting crystals. Together with the possibility to operate the systems remotely and fully autonomously with the SCOUT sample changer, the user experience closely resembles the experiences at a modern protein beamline, but with less time pressure plus the great benefit of the vicinity to the laboratory to facilitate experiment optimization.
While Default settings in our PROTEUM3 software enable also the non-expert user to generate excellent data in most cases, an optimized data collection on challenging systems is required to get the best data quality which can be crucial to solve the structure.
Here we will show how the properties of the X-ray beam delivered by focussing optics compares to those from synchrotron beamlines and how the experimental parameters must be considered differently to get the good data from poorly diffracting crystals with long unit cells.
