Scientific Research Division

Chun-Jung Chen (陳俊榮), Ph. D.

Research Scientist

Life Science Group

Office: Room S330, R&D Building

E-Mail: cjchen@nsrrc.org.tw, 

Tel: +886-35780281-7330

 

Education               

1994－1999  Ph.D. in Crystallography, University of Pittsburgh, U. S. A. 

1989－1991  M.S in Life Sciences, National Tsing Hua University, Taiwan

1985－1989  B.S in Physics, National Tsing Hua University, Taiwan

 

Employment

2011－ Research Scientist, Life Science Group, Scientific Research Division, NSRRC 

2011－ Joint Professor, Institute of Biotechnology, National Cheng Kung University

2011－ Joint Professor, Department of Physics, National Tsing Hua University

2013－ Visiting Professor, Department of Pharmaceutical Chemistry, King Saud University, Saudi Arabia

2004－2010 Associate Research Scientist, Life Science Group, Scientific Research Division, NSRRC

2008－2011 Joint Associate Professor, Department of Biotechnology, National Cheng Kung University

2005－2011 Joint Associate Professor, Department of Physics, National Tsing Hua University

2002－2005 Joint Assistant Professor, Department of Physics, National Tsing Hua University

2001－2002 Part-time Assistant Professor, Department of Physics, National Tsing Hua University

2001－2003 Assistant Research Scientist, Life Science Group, Research Division, NSRRC 

1999－2000 Post-doctoral Fellow, Department of Biochemistry and Molecular Biology, University of Georgia, U. S. A.

 

Research Interest

   My research fields include synchrotron X-ray protein crystallography, molecular biophysics, structural biology and proteomics. The major research interest is to study crystal structure and functional relationship of various proteins, including protein-DNA/RNA interaction, virus, membrane proteins, enzymes, and other functional important proteins related to drug discovery by Protein Crystallography (PX), X-ray Absorption Fine Structure (XAFS), Circular Dichroism (CD) and Small Angle X-ray Scattering (SAXS) using synchrotron X-rays from NSRRC and SPring-8. 

  Some primary targets include the important proteins and metalloproteins of sulphate-reducing bacteria to understand the life process mechanisms in anaerobic and aerobic environment; the proteins involved rice seed germination and coleoptile elongation; the membrane proteins account for the electron transfer chain, oxygen defencing system and drug targets. 

    In addition, many collaborative projects with domestic and international research institutes and universities have been carried out to study a number of proteins involved in diseases, medial application, drug design, venom toxicity, viral disease, catalysis, metabolism, etc. Another interest is to investigate the methodology for resolving the phase ambiguity of single-wavelength anomalous dispersion (SAD), which applies to obtain the correct phases routinely and efficiently for structure determination of macromolecules.

 

 

 

 

 

 

 

Selected Publication

 

1. Please refer the complete list at http://www.researcherid.com/rid/A-6880-2011

 

2. Crystal Structures of the Hydrolase Domain of Zebrafish 10-formyltetrahydrofolate Dehydrogenase and Its complexes reveal a complete set of key residues for hydrolysis and product inhibition. C.-C .Lin, P. Chuankhayan, W.-N. Chang, T.-T. Kao, H.-H. Guan, H.-K. Fun, A. Nakagawa, T.-F. Fu, and C.-J. Chen*, Acta Cryst. D71, 1006 (2015).  

 

3. Direct Phase Selection of Initial Phases from Single-Wavelength Anomalous Dispersion (SAD) for the Improvement of Electron Density and ab initio Structure Determination. C.-D. Chen, Y.-C. Huang, H.-L. Chiang, Y.-C. Hsieh, P. Chuankhayan, and C.-J. Chen*, Acta Cryst. D70, 2331 (2014).

 

4. Structural Insights into the Hydrolysis and Polymorphism of Methotrexate Polyglutamate by Zebrafish -Glutamyl Hydrolase. P. Chuankhayan, T.-T. Gao, , C.-C. Lin, H.-H. Guan, A. Nakagawa, A., T.-F. Fu, and C.-J. Chen*, J. Med. Chem. 56, 7625 (2013).

 

5. Crystal Structures of Vertebrate Dihydropyrimidinase and Complexes from Tetraodon nigroviridis with Lysine Carbamylation: Metal and Structural Requirements for Post-translational Modification and Function. Y.-C. Hsieh, M.-C. Chen, C.-C. Hsu, S. I. Chan, Y.-S. Yang, and C.-J. Chen*, J. Biol. Chem. 288, 30645 (2013).

 

6. Crystal Structures of Rice (Oryza sativa) Glyceraldehyde-3-phosphate Dehydrogenase Complexes with NAD+ and Sulfate Suggests Involvement of Phe37 in NAD+-specificity. Y.-C. Tien, P. Chuakhanyan, Y.-C. Huang, C.-D. Chen, J. Alikhajeh, S.-L. Chang, and C.-J. Chen*, Plant Mol. Biol. 80, 389 (2012).

 

7. Structural Insights into the Enzyme Catalysis from Comparison of Three Forms of Dissimilatory Sulfite Reductase from Desulfovibrio gigas. Y.-C. Hsieh, M.-Y. Liu, V. C.-C. Wang, Y.-L. Chiang, E.-H. Liu, W. Wu, S. I. Chan, and C.-J. Chen*, Mol. Microbiol. 78, 1101 (2010).

 

8. Crystal Structure and Mutational Analysis of Aminoacylhistidine Dipeptidase from Vibrio alginolyticus Reveal a New Architecture of M20 Metallopeptidases. C.-Y. Chang, Y.-C. Hsieh, T.-Y. Wang, Y.-C. Chen, Y.-K. Wang, T.-W. Chiang, Y.-J. Chen, C.-J. Chen*, and T.-K. Wu, J. Biol. Chem. 285, 39500 (2010).

 

9. Crystal Structures of Bacillus cereus NCTU2 Chitinase Complexes with Chitooligomers Reveal Novel Substrate Binding for Catalysis: a Chitinase without Chitin-binding and Insertion Domains. Y.-C. Hsieh, Y.-J. Wu, T.-Y. Chiag, C.-Y. Kuo, K. L. Shrestha, C.-F. Chao, Y.-C. Huang, P. Chuankhayan, W. Wu, Y.-K. Li, C.-J. Chen* J. Biol. Chem. 285, 31603 (2010).

 

10. Crystal Structures of Aspergillus japonicus fructosyltransferase Complex with Donor/Acceptor Substrates Reveal Complete Subsites in the Active Site for Catalysis. P. Chuankhayan, C.-Y.Hsieh, Y.-C. Huang, Y.-Y. Hsieh, H.-H. Guan, Y.-C. Hsieh, Y.-C. Tien, C.-D. Chen, C.-M. Chiang, and C.-J. Chen*, J. Biol. Chem. 285, 23249 (2010).