Imaging Proteins and Viruses at Atomic Resolution at NSRRC

Chun-Jung Chen^1,2,3,4*

¹Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu, Taiwan
²Department of Physics, National Tsing Hua University, Hsinchu, Taiwan
³Department of Biotechnology and Bioindustry Sciences, National Cheng Kung University, Tainan City, Taiwan
⁴Department of Biological Science and Technology, National Yang Ming Chaio Tung University, Hsinchu, Taiwan

* Presenter:Chun-Jung Chen, email:cjchen@nsrrc.org.tw

The National Synchrotron Radiation Research Center (NSRRC) is operating two synchrotron rings— the Taiwan Light Source (TLS) of 1.5 GeV since 1994 and the new Taiwan Photon Source (TPS) of 3 GeV with high brightness and low-emittance since 2016. Following the 7 phase I beamlines at TPS open to users in 2016, 9 phase II beamlines plus one PRT brain-imaging beamline are currently operational (6) or under commissioning/construction (4) open to users in 2021~2022, and another 9 phase III beamlines are initiated with construction starting from 2021.
The TPS provides great and new opportunities for advanced research on the various scientific fields, including biophysics and life sciences. Synchrotron protein crystallography (PX) has been effective for structure determination of biological macromolecules, especially the membrane proteins and large molecular assemblies, such as viruses. The highly bright X-ray provides the special needs for these relatively small or weak-diffraction crystals toward the atomic-resolution structures. The current advanced micro-beam PX beamline at TPS, together with TLS-operated and future TPS PX beamlines, more complicated and challenging structures of biological macromolecules can be resolved at high resolution.
In this talk, the current status and the future plan of PX facilities as well as biological-related beamlines of NSRRC are briefly introduced. Some recent applications of structural studies at atomic resolution on various viruses and membrane proteins with the crystals of the large unit cells and weakly diffraction benefited from synchrotron X-ray are also presented.

Keywords: X-ray crystallography, synchroton radiation, protein, virus, crystal structure