NSRRC Activity Report 2023

S ynchrotron macromolecular crystallography continues to be an irreplaceable tool for revealing the atomic structures of biomolecules, despite advancements in AI-based protein structure prediction ( e.g. , Alphafold and RoseTTAFold), cryogenic electron microscopy, and serial femtosecond crystallography. This method yields high-quality structures, crucial for understanding the intricate structure–activity relationship, which is fundamental for numerous scientific applications. The NSRRC supports this field with three dedicated protein beamlines— TLS 15A1 , TPS 05A , and TPS 07A —available to a wide user base. Additional specialized beamlines are offered to accommodate further research diversity, including those for small-angle X-ray scattering ( TPS 13A ), soft X-ray tomography ( TPS 24A ), transmission X-ray microscopy ( TPS 31A ), quick- scanning X-ray absorption spectroscopy ( TPS 44A ), white X-ray ( TLS 01A1 ), X-ray microscopy ( TLS 01B1 ), and infrared microspectroscopy ( TLS 14A1 ). In 2023, our user communities accomplished several remarkable scientific achievements. Consequently, in this activity report, we highlight four exceptional studies conducted using NSRRC facilities. The first study, conducted by Rey-Ting Guo, demonstrated how phosphoantigens serve as molecular glue, activating γδ T cells through structural interactions with BTN3A1 and BTN2A1. The second study, conducted by Che Ma and Chun-Hua Hsu, was a structural analysis of the SARS-CoV-2 spike protein, which uncovered the role of the receptor-binding domain and fusion core in cell entry, vaccine development, and discovery of monoclonal antibodies to neutralize various virus strains. The third study was by Chun-Jung Chen, who determined the structure of the Lake Sinai virus, a virus which infects honeybees, providing insight into viral assembly and infection mechanisms, which could aid in developing natural treatments for protecting bee colonies. Finally, the fourth study was by Tsung-Lin Li, who discovered Orf1, a noncanonical FAD-dependent enzyme that modifies aminoglycoside antibiotics, counteracting bacterial resistance by employing a unique ligand–enzyme NOS bridge mechanism, which could be instrumental in developing new antibiotics inhibiting acetylation by pathogenic bacteria. (by Chun-Hsiang Huang) Life Science