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	5.6-15.5
Wavelength (Å)	2.06-0.62	2.18-0.62	2.21-0.80
Aperture Size (µm) (types)*	100-2	200-10 (9)*	200-50 (5)*
Flux After Aperture (p/s)	820-86×1010	570-4.0×1010	14/8.5/3.7/2.2/1.0×1010
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

1. Cheng-Hung Chiang, Chung-Kuang Chou, Chien-Chang Tseng, Yi-Hui Chen, Yi-Chun Liu, Chen-Ying Huang, Chun-Hsiung Chao, and Chun-Hsiang Huang, Biopharmaceutical Beamline TLS 15A1 for Macromolecular Crystallography at the National Synchrotron Radiation Research Center. J. Chin. Chem. Soc. 2024, 71, [in press] [doi: 10.1002/jccs.202400111]


2. Yi-Hui Chen, Chien-Chang Tseng, Chung-Kuang Chou, Yi-Chun Liu, Cheng-Hung Chiang, Chen-Ying Huang, Chun-Hsiung Chao and Chun-Hsiang Huang, The highly efficient protein crystallography beamline TLS 13B1 at the National Synchrotron Radiation Research Center. J. Chin. Chem. Soc. 2023, 70(5), 1219. [doi: 10.1002/jccs.202300057]

1. Shen Wang, Chun-Hsiang Huang, et al., Structural basis for recruitment of peptidoglycan endopeptidase MepS by lipoprotein NlpI. Nat Commun. 2024, [doi: 10.1038/s41467-024-49552-y]


2. Chao-Yu Yang, Chia-I Lien, et al., Deciphering DED assembly mechanisms in FADD-procaspase-8-cFLIP complexes regulating apoptosis. Nat Commun. 2024, 15, 3791. [doi: 10.1038/s41467-024-47990-2]


3. Wesley Tien Chiang , Yao-Kai Chang, et al., Structural basis and synergism of ATP and Na+ activation in bacterial K+ uptake system KtrAB. Nat Commun. 2024, 15, 3850. [doi: 10.1038/s41467-024-48057-y]


4. Eric Y C Mao, Han-Yi Yen, Chyuan-Chuan Wu, Structural basis of how MGME1 processes DNA 5' ends to maintain mitochondrial genome integrity. Nucleic Acids Research. 2024, 52, 4067. [doi: 10.1093/nar/gkae186]


5. Chen-Hsi Chu, Che-Ting Wu,et al. , Insights into the molecular mechanism of ParABS system in chromosome partition by HpParA and HpParB. Nucleic Acids Research. 2024, 1. [doi: 10.1093/nar/gkae450]


6. Manuel Maestre-Reyna et al. Visualizing the DNA repair process by a photolyase at atomic resolution. Science. 2023, 382, eadd7995. [doi: 10.1126/science.add7795]


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


8. Huang, KY.A., Chen, X., Mohapatra, A. et al. Structural basis for a conserved neutralization epitope on the receptor-binding domain of SARS-CoV-2. Nat Commun. 2023,14 ,311. [doi: 10.1038/s41467-023-35949-8]


9. Chen, NC., Wang, CH., Yoshimura, M. et al. Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions. Nat Commun. 2023, 14, 545. [doi: 10.1038/s41467-023-36235-3]


10. Nguyen, H.T.V., Chen, X., Parada, C. et al. Structure of the heterotrimeric membrane protein complex FtsB-FtsL-FtsQ of the bacterial divisome. Nat Commun. 2023, 14, 1903. [doi: 10.1038/s41467-023-37543-4]


11. Wang, YL., Chang, CY., Hsu, NS. et al. N-Formimidoylation/-iminoacetylation modification in aminoglycosides requires FAD-dependent and ligand-protein NOS bridge dual chemistry. Nat Commun. 2023, 14, 2528. [doi: 10.1038/s41467-023-38218-w]