About NSRRC / Staff Directory

Life Science Group


Name： 陳俊榮( Chun-Jung Chen )
EXT.： 7330
E-mail： cjchen@nsrrc.org.tw
Website： http://bionsrrc.nsrrc.org.tw/
Education：
  • B.S., Physics Department, National Tsing-Hua University, Taiwan (1985-1989)
  • M. S., Institute of Life Sciences, National Tsing-Hua University, Taiwan (1989-1991)
  • Ph. D., Department of Crystallography, University of Pittsburgh, U. S. A. (1994-1999)
Experience：
  • Council Member, International Union of Crystallography (2022/06~)
  • Chairman, The Crystallographic Committee, Academia Sinica, Taipei, R.O.C. (2022/06~)
  • Council Member, Division of Physical Biology and Biological Physics (PBBP) of TPS (2022/02~)
  • Chairman, Taiwan Crystallographic Group (2021~)
  • Deputy Director (2018/08~2022/07)
  • Division Head, Scientific Research Division (2016/07~2018/07)
  • Division Head, Scientific Research Division (2012/07~2014/06)
  • Scientist, Life Science Group, Scientific Research Division, NSRRC (2011/01~)
  • Joint Professor, Dept. of Biological Science & Technology, National Yang Ming Chiao Tung University (2019/08~)
  • Joint Professor, Graduate Inst. of Applied Science and Technology, National Taiwan University of Science and Technology (2019/08~)
  • Joint Professor, Dept. of Biotechnology and Bioindustry Sciences, National Cheng Kung University (2011/08~)
  • Joint Professor, Dept. of Physics, National Tsing Hua University (2011/08~)
  • Associate Scientist, Life Science Group, Research Division, NSRRC (2004/01-2010/12)
  • Joint Associate Professor, Institute of Biotechnology, National Cheng Kung University (2008/08~2011/07)
  • Joint Associate Professor, Dept. of Physics, National Tsing Hua University (2005/08~2011/07)
  • Joint Assistant Professor, Dept. of Physics, National Tsing Hua University (2002/08-2005/07)
  • Part-time Assistant Professor, Dept. of Physics, National Tsing Hua University (2001/08-2002/07)
  • Assistant Scientist, Biology Group, Research Division, NSRRC (2001/01-2003/12)
  • Postdoctoral fellow, Dept. of Biochemistry & Molecular Biology, Univ. of Georgia, U.S.A. (1999/12-2000/10)
Endstation：
  • Laboratory of Protein Crystallography and Structural Biology
  • TPS 07A
  • SPring-8 BL44XU
Research Interests：

  • My research fields range from synchrotron X-ray protein crystallography to molecular biophysics, structural biology and biochemistry. The major research interest aims to study the structure and functional relationship of various proteins and biological assemblies, including viruses, membrane proteins, protein-DNA/RNA interactions, enzymes, and other functional important proteins related to diseases and drug discovery by protein crystallography (PX), X-ray absorption fine structure (XAFS), circular dichroism (CD), small angle scattering (SAS) and Infarred spectra (IR) using synchrotron light source from NSRRC and SPring-8. In addition, we combines the X-ray methods with Cryo-EM as a complementary approach to measure the structures of biological macromolecular assemblies.

    In recent years and in the future, the research focuses on the structural and functional relationships between important membrane proteins, viruses, protein and nucleic acid complexes, as well as a long-term cooperation with the biotechnology industry for new drug development.

    Some specific targets are: the important membrane proteins and metalloproteins of sulfate-reducing bacteria to understand the life process mechanisms in anaerobic and aerobic environment; the proteins involved in cancer development and diseases; various viruses to elucidate the mechanisms of particle assembly and viral infection;  the membrane proteins accounting for the electron transfer chain, oxygen defense 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, medical application, drug design, venom toxicity, viral disease, catalysis, metabolism, etc. Another interest focuses on investigating the methodology for resolving the protein crystallization and phase problem in protein crystallography, which applies to obtain the correct phases routinely and efficiently for structure determination of biological macromolecules.
Selected Publications： For the complete list, please go to https://www.researchgate.net/profile/Chun-Jung_Chen2 or https://scholar.google.com.tw/citations?hl=zh-TW&user=oTFF8K0AAAAJ&view_op=list_works&sortby=pubdate or https://orcid.org/0000-0002-5157-4288
  • Chen, N.-C., Wang, C.-H., Yoshimura, M., Yeh, Y.-Q., Guan, H.-H., Chuankhayan, P., Lin, C.-C., Lin, P.-J., Huang, Y.-C., Wakatsuki, S., Ho, M.-C.*, Chen, C.-J.* “Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions” Nature Commun. 14: 545 (2023).
  • Chuankhayan, P., Lee, R.-H., Guan, H.-H., Lin, C.-C., Chen, N.-C., Huang, Y.-C., Yoshimura, M., Nakagawa, A., Chen, C.-J.* “Structural insight into the hydrolase and synthase activities of an alkaline α-galactosidase from Arabidopsis from complexes with substrate/product”. Acta Cryst. D79, 154–167 (2023).
  • Chan, S. I.*, Chuankhayan, P., Nareddy, Pavan K., Tsai, I-K., Tsai, Y.-F., Chen, K. H.-C., Yu, S. S.-F.*, Chen, C-J.* “The mechanism of PQQ-dependent hydride transfer chemistry from spectroscopic and high-resolution X-ray structural studies of the methanol dehydrogenase from Methylococcus capsulatus (Bath)” J. Am. Chem. Soc. 143, 9, 3359-3372 (2021)
  • Guan, H. H., Huang, Y. H., Lin, E. S., Chen, C.-J.*, & Huang, C. Y.* “Plumbagin, a natural product with potent anticancer activities, binds to and inhibits dihydroorotase, a key enzyme in pyrimidine biosynthesis” Intl. J. Mol. Sci. 22(13), 6861 (2021)
  • Chen, S.-K. Guan, H.-H., Wu, P.-H., Lin, L.-T., Wu, M.-C., Chang, H.-Y., Chen, N.-C., Lin, C.-C., Chuankhayan, C., Huang, Y.-C., Lin, P.-J., Chen, C.-J.* “Structural insights into histidine-containing phosphotransfer protein and receiver domain of sensor histidine kinase suggest a complex model in two-component regulatory system in Pseudomonas aeruginosa” IUCrJ, 7, 934-948 (2020).
  • Yoshimura, M., Chen, N.-C., Guan, H.-H., Chuankhayan, P., Lin, C.-C., Nakagawa, A., Chen, C.-J.* "Non-crystallographic symmetry constraint map obtained by direct density optimization" Acta Cryst. D76, 147-154 (2020).
  • Chen, N.-C., Yoshimura, Naoyuki Miyazaki, M.Guan, H.-H., Chuankhayan, P., Lin, C.-C., Chen, S.-K., Lin, P.-J., Huang, Y.-C., Iwasaki, K., Nakagawa, A., Chan, S. I., Chen, C.-J.* “The atomic structures of shrimp nodaviruses reveal new dimeric spike structures and particle polymorphism” Commun. Biol. 2:72 (2019).
  • Guan, H.-H., Hsieh, Y.-C., Lin, P.-J., Huang, Y.-C. Yoshimura, M., Chen, L.-Y., Chen, S.-K., Chuankhayan, P., Lin, C.-C., Chen, N.-C., Nakagawa, A., Chan, S. I., Chen, C.-J.* “Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas”, Sci. Rep. 8:14935 (2018).
  • Chen, L.-Y., Huang, Y.-C., Huang, S.-T., Hsieh, Y.-C., Guan, H.-H., Chen, N.-C., Chuankhayan, P., Yoshimura, M., Tai, M.-H., Chen, C.-J.* “Domain swapping and SMYD1 interactions with the PWWP domain of human hepatoma-derived growth factor” Sci. Rep. 8(1): 287 (2018).
  • Huang, Y.-H., Guan, H.-H., Chen, C.-J.*, Huang, C.-Y. “Staphylococcus aureus single-stranded DNA-binding protein SsbA can bind but cannot stimulate PriA helicase. PLoS ONE, 12, e0182060 (2017).
  • Yoshimura, M., Chen, N.-C., Guan, H.-H., Chuankhayan, P., Lin, C.-C., Nakagawa, A., Chen, C.-J.* “Ab initio phasing by molecular averaging in real space with new criteria: application to structure determination of a betanodavirus” Acta Cryst. D72, 830-840 (2016).
  • Chiu, H.-H., Hsieh, Y.-C., Chen, Y.-H., Wang, H.-Y., Lu, C.-Y., Chen, C.-J.*, Li, Y.-K. "Three important amino acids control the regioselectivity of flavonoid glucosidation in glycosyltransferase-1 from Bacillus cereus" Appl. Microbiol. Biotechnol. 100, 8411-8422 (2016).
  • Guan, H.-H. Yoshimura, M., Chuankhayan, P., Lin, C.-C., Chen, N.-C., Yang, M.-C., Ismail, A., Fun, H.-K., Chen, C.-J.* Crystal structure of an antigenic outer-membrane protein from Salmonella Typhi suggests a potential antigenic loop and an efflux mechanism” Sci. Rep. (Nature Publishing Group), 5:16441 (2015).
  • Chen, N.-C., Yoshimura, M., Guan, H.-H., Wang, T.-Y., Misumi, Y., Lin, C.-C., Chuankhayan, P., Nakagawa, A., Chan, S. I., Tsukihara, T., Chen, T.-Y., Chen, C.-J.* “Crystal structures of a piscine betanodavirus: mechanisms of capsid assembly and viral infection” PLoS Path. 11(10): e1005203 (2015).
  • Chen, K. H.-C., Chuankhayan, C., Wu, H.-H., Chen, C.-J.*, Fukuda, M., Yu, S. S.-F., Chan, S. I. "The bacteriohemerythrin from Methylococcus capsulatus (Bath): Crystal structures reveal Leu114 regulates the substrate tunnel" J. Inorg. Biochem. 15, 81-89 (2015).
  • Lin, C.-C., Chuankhayan, P., Chang, W.-N., Kao, T.-T., Guan, H.-H., Fun, H.-K., Nakagawa, A., Fu, T.F., Chen, C.-J.* “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”, Acta Cryst. D71. 1006-1021 (2015).
  • Chen, C.-D., Huang, Y.-C., Chiang, H.-L., Hsieh, Y.-C., Chuankhayan, P., Chen, C.-J.* “Direct phase selection of initial phases from single-wavelength anomalous dispersion (SAD) for the improvement of electron density and ab initio structure determination” Acta Cryst. D70, 2331-2343 (2014).
  • Praditwongwan, W, Chuankhayan, P., Saoin, S., Wisitponchai, T., Lee, V. S., Nangola, S., Hong, S. S., Minard, P., Boulanger, P., Chen, C.-J.*, Tayapiwatana, C. “Crystal structure of an antiviral ankyrin targeting the HIV-1 capsid and molecular modeling of the ankyrin-capsid complex” J. Comput. Mol. Des. 28, 869-884 (2014).
  • Chuankhayan, P., Tao, T.-T., Lin, C.-C., Guan, H.-H., Nakagawa, A., Fu, T.-F., Chen, C.-J.* “Structural insights into the hydrolysis and polymorphism of methotrexate polyglutamate by zebrafish γ-glutamyl hydrolase” J. Med. Chem. 56, 7625-7635 (2013).
  • Hsieh, Y.-C., Chen, M.-C., Hsu, C.-C., Chan, S. I., Yang, Y.-S., Chen, C.-J.* “Crystal structures of vertebrate dihydropyrimidinase and complexes from Tetraodon Nigroviridis with lysine carbamylation: metal and structural requirements for post-translational modification and function” J. Biol. Chem. 288, 30645-30658 (2013).
  • Tien, Y.-C., Chuakhanyan, P., Huang, Y.-C., Chen, C.-D., Alikhajeh, J., Chang, S.-L., Chen, C.-J.* “Crystal structures of rice (Oryza sativa) glyceraldehyde-3-phosphate dehydrogenase complexes with NAD+ and sulfate suggests involvement of Phe37 in NAD+-specificity”. Plant Mol.Biol. 80, 389-403 (2012).
  • Chen, C.-D., Lin, C.-H., Chuankhayan P., Huang, Y.-C., Hsieh, Y.-C., Huang, T.-F., Guan, H.-H., Liu, M.-Y., Chang, W.-C., Chen, C.-J.* “Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with α-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis”. J Bacteriol. 194, 6206-6216 (2012).
  • Fang, J.-Y., Chiang, Y.-L., Hsieh, Y.-C., Wang, V. C.-C., Huang, Y.-C., Chuankhayan, P., Liu, M.-Y., Chan, S. I., Chen, C.-J.* “Crystallization of adenylylsulfate reductase from Desulfovibrio gigas: A strategy based on controlled protein oligomerization” Cryst. Growth & Des. 11, 2121-2134 (2011).
  • Hsieh, Y.-C., Liu, M.-Y., Wang, V. C.-C., Chiang Y.-L., Liu, E.-H., Wu, W., Chan, S. I., Chen, C.-J.* “Structural insights into the enzyme catalysis from comparison of three forms of dissimilatory sulfite reductase from Desulfovibrio gigas” Mol. Microbiol. 78, 1101-1116 (2010).
  • Chang, C.-Y., Hsieh, Y.-C., Wang, T.-Y., Chen, Y.-C., Wang Y.-K., Chiang, T.-W., Chen, Y.-J., Chen, C.-J.*, Wu, T.-K. “Crystal structure and mutational analysis of aminoacylhistidine dipeptidase from Vibrio alginolyticus reveal a new architecture of M20 metallopeptidases”, J. Biol. Chem. 285, 39500-39515 (2010).
  • Hsieh, Y.-C., Wu, Y.-J., Chiag, T.-Y., Kuo, C.-Y., Shrestha, K. L., Chao, C.-F., Huang, Y.-C., Chuankhayan, P., Wu, W., Li, Y.-K., Chen, C.-J.* “Crystal structures of Bacillus cereus NCTU2 chitinase complexes with chitooligomers reveal novel substrate binding for catalysis: a chitinase without chitin-binding and insertion domains” J. Biol. Chem. 285, 31603-31615 (2010).
  • Chuankhayan, P., Hsieh, C.-Y., Huang, Y.-C., Hsieh, Y.-Y., Guan, H.-H., Hsieh, Y.-C., Tien, Y.-C., Chen, C.-D., Chiang, C.-M., Chen, C.-J.* “Crystal structures of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete subsites in the active site for catalysis” J. Biol. Chem. 285, 23249-23262 (2010).
  • Guan, H.-H. Guan, Goh, K.-S., Davamani, F., Wu, P.-L., Huang, Y.-W., Jeyakanthan, J., Wu, W., Chen, C.-J.* “Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins”, J. Struct. Biol. 169, 294-303 (2010).
  • Chiang, Y.-L., Hsieh, Y.-C., Fang, J.-Y., Liu, E.-H., Huang, Y.-C., Chuankhayan, P., Jeyaraman, J., Liu, M.-Y., Chan, S. I., Chen, C.-J.* “Crystal structure of adenylylsulfate reductase from Desulfovibrio gigas suggests a potential self-regulation mechanism involving the C-terminus of the β-subunit”. J. Bacteriol. 191, 7597-7608 (2009).
  • Yang, M.-C., Guan, H.-H., Liu, M.-Y., Lin, Y.-H., Yang, J.-M., Chen, W.-L., Chen, C.-J.*, Mao, S.J.T. “Rational design for crystallization of b-Lactoglobulin and vitamin D3 complex: revealing a secondary binding site”, Cryst. Growth and Des. 8, 4268-4276 (2008).
  • Yang, M.-C., Guan, H.-H., Liu, M.-Y., Lin, Y.-H., Yang, J.-M., Chen, W.-L., Chen, C.-J.*, Mao, S.J.T. “Crystal structure of a secondary vitamin D3 binding site of milk b-lactoglobulin”, Proteins, 71, 1197-1210 (2008).
  • Elmi, F., Lee, H.-T., Huang, J.-Y., Hsieh, Y.-C., Wang, Y.-L., Chen, Y.-J., Shaw, S.-Y., Chen C.-J.* “Stereoselective esterase from Pseudomonas putida reveals an a/b hydrolase fold for D-b acetylthioisobutyric acid synthesis”, J. Bacteriol. 187, 8470-8476 (2005).
  • Huang, J.-Y, Chang, T, Chang, C.-Y., Chen, C.-J.* “Crystal structure of a nucleoside diphosphate kinase required for coleoptile elongation in rice (Oryza sativa L.)”, J. Strut. Biol. 150, 309-318 (2005).
  • Lee, S.-C., Guan, H.-H., Wang, C.-H., Huang, W.-N., Chen, C.-J.*, and Wu, W. “Structural basis of venom citrate-dependent heparan sulfate-mediated cell surface retention of cobra cardiotoxin A3”. J. Biol. Chem. 280, 9567-9577 (2005).