The core technique of our facility is Synchrotron Radiation Protein Crystallography, a technique that uses the principle of single crystal X-ray diffraction to determine high-resolution three-dimensional protein molecular structure from a protein crystal. It is the most powerful and important method to study biological structures. Currently, nine out of every ten biological structures are solved by this technique. Worldwide, only 18 countries and the European Union possess synchrotron radiation facilities and provide protein crystallography technique, and Taiwan is included. Being the only facility in Taiwan that provides this technique, our goal is to build a world-class protein crystallographic facility to assist industrial and academic scientists and experts in the field of biomedical science (including structural biology, proteomics, biochemistry, molecular biology, drug design, biotechnology, etc.) to develop prevention, diagnosis, and treatment of various diseases. That helps improve the health of people, increase the quality of life and effectively conserve medical resources.

NSRRC PX Beamline	TPS 07A Micro-focus Protein Crystallography	TPS 05A Protein Microcrystallography	TLS 15A1 Biopharmaceutical Protein Crystallography
X-ray source	TPS/ 3 GeV/ Undulator	TPS/ 3 GeV/ Undulator	TLS/ 1.5 GeV/ Wiggler
General user time	70%	75%	80%
Status	Operational	Operational	Operational
Experiment	MAD/Micro-focus beam	MAD/Microbeam	MAD
Energy range (keV)	6.0-20.0	5.7-20.0	7.0-15.5
Wavelength (Å)	2.06-0.62	2.18-0.62	1.77-0.80
Aperture Size (µm) (types)*	100-2	200-10 (9)*	200-50 (5)*
Flux After Aperture (p/s)	820-86×1010	570-4.0×1010	12/9/4/2/1.1×1010
Flux Density (phots/s/µm2)	9.4-1600×108	1.8-5.0×108	5.7-7.5×106
Time to Henderson Limit (s)	0.24-42.6	12.1-15.4	5333-7018
Detector	EIGER2 X 16M	EIGER2 X 9M	MX300HE
Frame Rate (frames/s)	130 Hz	230 Hz	1
Sample Changer	ISARA	ISARA	SAM
Remote Access	YES	YES	YES

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2. Yuan, L., Ma, X., Yang, Y. et al. Phosphoantigens glue butyrophilin 3A1 and 2A1 to activate Vγ9Vδ2 T cells. Nature. 2023, 621, 840-848. [doi: 10.1038/s41586-023-06525-3]


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7. Yang, CS., Ko, TP., Chen, CJ. et al. Crystal structure and functional implications of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases. Nat Commun.2023, 14, 5078. [doi: 10.1038/s41467-023-40787-9]


8. Roshan Satange, Chih-Chun Chang, Long-Yuan Li, Sheng-Hao Lin, Stephen Neidle, Ming-Hon Hou, Synergistic binding of actinomycin D and echinomycin to DNA mismatch sites and their combined anti-tumour effects. Nucleic Acids Research. 2023, 51 (8), 3540-3555. [doi: 10.1093/nar/gkad156]


9. Kuan-Wei Huang, Chia-Yun Wu, Shu-Ing Toh, Tung-Chang Liu, Chun-I Tu, Yin-Hsin Lin, An-Ju Cheng, Ya-Ting Kao, Jhih-Wei Chu, Yu-Yuan Hsiao, Molecular insight into the specific enzymatic properties of TREX1 revealing the diverse functions in processing RNA and DNA/RNA hybrids. Nucleic Acids Research. 2023, 51, 11927-11940. [doi: 10.1093/nar/gkad910]


10. Salila Pengthaisong, Beatriz Piniello, Gideon J. Davies, Carme Rovira* and James R. Ketudat Cairns, Reaction Mechanism of Glycoside Hydrolase Family 116 Utilizes Perpendicular Protonation. ACS Catal. 2023, 13, 5850-5863. [doi: 10.1021/acscatal.3c00620]