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Synchrotron protein crystallography (PX) remains an indispensable tool for uncovering the atomic structures of biomolecules. TLS 15A1, operated by the protein diffraction group of NSRRC, has been accessible to both academic and industrial users since January 2013. This beamline is energy‐tunable within a range between 5.6 and 15.5 keV, which is suitable for phasing experiments. Over the past 11 years, TLS 15A1 has supported 657 projects and facilitated 1523 experiments across 41,656 h of beamtime. This article describes the beamline layout, studies of factors influencing data quality, and significant scientific contributions. Photograph of the sample environment set‐up in the TLS 15A1 experimental station. The experimental station is equipped with a high precision X‐ray MD2 micro‐diffractometer, a large area CCD detector, Cryojet, and an automatic sample mounting system (SAM) for highly efficient data collection.

Synchrotron protein crystallography (PX) is one of the most powerful and dominant tools for determining the three‐dimensional structures of biological macromolecules. At the National Synchrotron Radiation Research Center, TLS 13B1 is the first dedicated energy‐tunable and highly automated PX beamline for efficiently solving de novo protein structures in Taiwan and has been open for users since September 2005. With remote access, user support services, and annual PX training courses over 17 years, the number of user groups at TLS 13B1 has grown from 11 to 139. In total, 1,429 projects were supported, and 2090 experiments were hosted during 67,846 hr of beamtime. This paper describes the photon source, beamline components, experimental station equipment, beamline software, beamline application process, and results from our users. Photograph of the sample environment setup in the TLS 13B1 experimental station. The experimental station is equipped with a high‐precision X‐ray MD2 micro‐diffractometer, a large area CCD detector, Cryojet, and an automatic sample mounting system (SAM) for highly efficient data collection.