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ABSTRACT

BM07 is a French CRG beamline dedicated to macromolecular crystallography experiments, built during the EBS shutdown as a successor to BM30A, which was originally developed as a tuneable energy beamline to determine structures using anomalous signal-based techniques. With the advent of AI-based methods to determine protein structure de novo, BM07 has initially focussed on optimising high-throughput screening of crystals maintained at cryogenic temperature, and subsequent diffraction data collection. Besides, the beamline now offers a portfolio of different techniques to study protein dynamics, thanks to a new versatile goniometer. This includes data collection at different energies (6.5 – 20 keV), at various temperatures (from 80 to 333 K), under variable hydrostatic pressure (up to 50 kbar), and the use of UV-visible absorption and fluorescence emission spectroscopy as a complementary optical spectroscopy technique directly applied to the crystal placed on the diffractometer. Last, time-resolved crystallography experiments can be performed on the second to minute timescale using either liquid substrate/cofactor dispensing or light activation in order to initiate reactions in enzymes or photosensitive proteins.