About Us

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.


Protein Crystallography Beamline Information

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

Beamline Publications

  1. Chung-Kuang Chou, Chien-Chang Tseng, Cheng-Hung Chiang, Yi-Hui Chen, Yi-Chun Liu, Chen-Ying Huang, Chun-Hsiung Chao and Chun-Hsiang Huang, The current status and future prospects of the Synchrotron Radiation Protein Crystallography Core Facility at NSRRC: a focus on the TPS 05A, TPS 07A and TLS 15A1 beamlines. J. Synchrotron Rad. 2025, 32(2), 457. [doi: 10.1107/S1600577525000177]

  2. 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(7), 721. [doi: 10.1002/jccs.202400111]

  3. 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]


User Publications (High Impact Factor)

  1. Lu-Yi Chen et al., Mesostructured Water Enhances Stability of ProteinMPNN-Designed Ubiquitin-Fold Proteins. Journal of the American Chemical Society 2026, 148(7), 7363-7377. [doi: 10.1021/jacs.5c19875]

  2. Tsan-Jan Chen et al., GSH as an A-A Type Allosteric Activator of PKM2: Modulating Cancer Cell Homeostasis and Ferroptosis Susceptibility. Advanced Science 2026, 13(5), e19368. [doi: 10.1002/advs.202519368]

  3. Kuan-Wei Huang et al., Disordered DNA-binding motif forms a modulation site for inhibiting the cancer immunotherapy target TREX1. Nucleic Acids Research 2026, 54(2), gkaf1511. [doi: 10.1093/nar/gkaf1511]

  4. Cheng-Chung Lee et al., Structural basis of B-to-Z DNA transition mediated by an anti-Z-DNA antibody. Nucleic Acids Research 2026, 54(5), gkag160. [doi: 10.1093/nar/gkag160]

  5. Chanisara Kaewsasan et al., Capturing Catalysis: Structural Insights into the Acyl-Enzyme Intermediate of Priestia megaterium Penicillin G Acylase. ACS Catalysis 2026, (in press). [doi: 10.1021/acscatal.6c00015]

  6. Sheng-Chia Chen et al., Structural and functional insights into an archaeal dUTPase reveal a subdomain-mediated mechanism for substrate recognition and evolutionary adaptation. International Journal of Biological Macromolecules 2026, 335(1), 149194. [doi: 10.1016/j.ijbiomac.2025.149194]

  7. Yu-Hung Chen et al., Structural insights into substrate binding, domain swapping and heat resistance of a hyperthermostable archaeal AIR synthetase. International Journal of Biological Macromolecules 2026, 344(1), 150493. [doi: 10.1016/j.ijbiomac.2026.150745]

  8. Rawiporn Amornloetwattana et al., Cellular Upcycling of Polyethylene Terephthalate (PET) With an Engineered Human Saliva Metagenomic PET Hydrolase. ChemSusChem 2026, 19(1), e202502560. [doi: 10.1002/cssc.202502560]

  9. Jie Yang, Pei-Fen Liu et al., Salt bridge disruption in colicin Ib channel-forming domain enhances membrane translocation and bactericidal activity. Journal of Structural Biology: X 2026, 13, 100144. [doi: 10.1016/j.yjsbx.2026.100144]

  10. Sheng-Han Hsu et al., Circular Permutation of the E. coli Heat-Labile Enterotoxin Pentameric B Subunit for Mucosal Vaccine Adjuvant Design. ACS Omega 2026, 11(5), 8784-8798. [doi: 10.1021/acsomega.5c12660]

  11. Kanyarat Suksomjaisaman et al., Structure and reaction mechanisms of a two-component indole monooxygenase from Acinetobacter baumannii. Arch Biochem Biophys. 2026, 776, 110681. [doi: 10.1016/j.abb.2025.110681]