Dr. Joseph D. Ng
The goal of our laboratory is to elucidate the structure and function of proteins involved in the passage of genetic information. We are developing and utilizing the combined techniques of Molecular Biology, Protein Chemistry, and X-ray and Neutron Crystallography to decipher the molecular mechanism and action of specific hyperthermophilic proteins. Strategies and tools for the rapid construction of new protein complexes are valuable for biotechnology applications. Our studies include the design and engineering of macromolecular systems for DNA replication using gene synthesis and structural biology tools.
Kuznetsov, Y.G., Dowell, J.J., Gavira, J.A., Ng, J.D. and McPherson A. (2010). Biophysical and atomic force microscopy characterization of the RNA from setellite tobacco mosaic virus. Nucleic Acids Res. (In Press).
Kantardjieff, K.A., Lind, C., Ng, J.D. and Santarisiero B.D. (2010) Efforts to enhance coverage of crystallography in United States scecondary education. J. Appl. Cryst. 43:1181-1188.
Tomanicek, S.J., Hughes, R.C., Ng, J.D. and Coates, L. (2010). Structure of endonuclease IV homologue from Thermotoga maritima in the presence of active-site divalent metal ions. Acta Crystallogr Section F Structural Biol Cryst. Commun 66:1003-1012.
Hughes, R.C., Tomanicek, S.J., Ng, J.D. and Coates, L. (2009). Purification, crystallization and preliminary crystallographic analysis of a thermostable endonuclease IV from Thermotoga maritima. Acta Crystallogr Sect F Struct Biol Cryst Commun.65:1317-1319.
Otálora, F., Gavira, J.A., Ng, J.D. and García-Ruiz J.M. (2009). Counterdiffusion methods applied to protein crystallization. Prog Biophys Mol Biol. 101:26-37.
Byrne-Steele, M.L., Hughes, R.C. and Ng, J.D. (2009). Recombinant production, crystallization and preliminary X-ray analysis of PCNA from the psychrophilic archaeon Methanococcoides burtonii DSM 6242. Acta Crystallogr Sect F Struct Biol Cryst Commun.65:1131-1135.
Byrne-Steele, M.L. and Ng, J.D. (2009). Expression, purification and preliminary X-ray analysis of proliferating cell nuclear antigen from the archaeon Thermococcus thioreducens. Acta Crystallogr Sect F Struct Biol Cryst Commun.65:906-909.
Wilson, R.C., Hughes, R.C., Flatt, J.W., Meehan, E.J. and Ng, J.D. and Twigg, P.D. (2009). Structure of full-length ubiquitin-conjugating enzyme E2-25K (huntingtin-interacting protein 2). Acta Crystallogr Sect F Struct Biol Cryst Commun.65:440-444.
Marsic, D., Flaman, JM and Ng, J.D. (2008). New DNA polymerase from the hyperthermophilic marine archaeon Thermococcus thiroreducens. Extremophiles 12:775-788.
Marsic, D., Hughes, RC, Byrne-Steele, M.L. and Ng, J.D. (2008). PCR-based gene synthesis to produce recombinant proteins for crystallization. BMC Biotechnology. 8:44.
Ng, J.D., Stevens, R.C. Clark P. and Kuhn P. (2008). In situ X-ray analysis of proteins crystals in low birefringent and X-ray transmissive plastic micro-channels. Acta Crystallogr D Biol Crystallogr D64:189-197.
Ng, J.D., Stevens, R.C. and Kuhn P. (2008). Protein crystallization in restricted geometry: advancing old ideas for modern times in structural proteomics. Methods in Molecular Biology 426:363-376.
Baird, J.K., Caraballo, K. and Ng, J.D. (2007). Kinetics of protein crystallization. Book Chapter in Focus on Crystal Growth Research (Ed: G.V. Karas) pp 171-192.
Wilson, R.C., Hughes, R.C., Curto, E.V., Ng, J.D. and Twigg, P.D. (2007). Backbone 1H, 15N, and 13C Resonance Assignments and Secondary Structure of a Novel Protein OGL-20PT-358 from
Hyperthermophile Thermococcus thioreducens sp. nov.Molecules and Cells 24:437-440.
Hughes, R. and Ng, J.D. (2007). Can small laboratories do structural genomics? Crystal Growth and Design 7:2226-2238.
Shaw, N., Tempel W, Chang, J., Yang, H., Cheng, C., Ng, J.D., Rose, J., Rao, Z. Wang, B.C. Liu, Z.J, (2007). Crystal structure solution of a ParB-like nuclease at atomic resolution. Proteins 70:263-267.
Shaw, N. Cheng, C., Tempel, W. Chang, J. Ng, J.D., Wang, XY, Perrett, S., Rose, J., Rao, Z., Wang, B.C. and Liu, ZJ. (NZ)CH...O contacts assist crystallization of a ParB-like nuclease. BMC Struct. Biol. 7:46.
Pikuta, E., Marsic, D., Itoh, T., Bej, A.K., Tang, J., Whitman, W., Ng, J.D., Garriott, O.K. and Hoover, R.B. (2007). Thermococcus thioreducens sp. nov., a novel hyperthermophilic, obligately sulfur-reducing archaeon from a deep-sea hydrothermal vent. Int. J Syst Evol Microbiol. 57:1612-1618.
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