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
Biopharmaceuticals 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

Publications (High Impact Factor)

  1. 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]

  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]

  3. 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]

  4. 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]

  5. 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]

  6. 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]

  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]