Venu Gopal Vandavasi
  • Biology and Soft Matter Division, Oak Ridge National Laboratory, USA
Research fields
  • Plant science
Personal information


Ph.D in Biotechnology & Biophysics from Saha Institute of Nuclear Physics, Kolkata, India

Current position

ORAU Post-doctoral Research Associate at Oak Ridge National Laboratory, Oak Ridge, TN, USA


  1. Vandavasi, V. G., Weiss, K. L., Cooper, J. B., Erskine, P. T., Tomanicek, S. J., Ostermann, A., Schrader, T. E., Ginell, S. L. and Coates, L. (2016). Exploring the Mechanism of beta-Lactam Ring Protonation in the Class A beta-lactamase Acylation Mechanism Using Neutron and X-ray Crystallography. J Med Chem 59(1): 474-479.

  2. Vandavasi, V. G., Putnam, D. K., Zhang, Q., Petridis, L., Heller, W. T., Nixon, B. T., Haigler, C. H., Kalluri, U., Coates, L., Langan, P., Smith, J. C., Meiler, J. and O'Neill, H. (2016). A Structural Study of CESA1 Catalytic Domain of Arabidopsis Cellulose Synthesis Complex: Evidence for CESA Trimers. Plant Physiol 170(1): 123-135.

  3. McFeeters, H., Vandavasi, V. G., Weiss, K. L., Coates, L. and McFeeters, R. L. (2016). Neutron diffraction analysis of Pseudomonas aeruginosa peptidyl-tRNA hydrolase 1. Acta Crystallogr F Struct Biol Commun 72(Pt 3): 220-223.

  4. Nixon, B. T., Mansouri, K., Singh, A., Du, J., Davis, J. K., Lee, J. G., Slabaugh, E., Vandavasi, V. G., O'Neill, H., Roberts, E. M., Roberts, A. W., Yingling, Y. G. and Haigler, C. H. (2016). Comparative Structural and Computational Analysis Supports Eighteen Cellulose Synthases in the Plant Cellulose Synthesis Complex. Sci Rep 6: 28696.

  5. Coates, L., Cuneo, M., Frost, M., He, H., Weiss, K., Tomanicek, S. and Vandavasi, V. G. (2015). The Macromolecular Neutron Diffractometer MaNDi at the Spallation Neutron Source. J Appl Crystallogr 48(4): p1302.

  6. Vandavasi, V., Taylor-Creel, K., McFeeters, R. L., Coates, L. and McFeeters, H. (2014). Recombinant production, crystallization and X-ray crystallographic structure determination of peptidyl-tRNA hydrolase from Salmonella typhimurium. Acta Crystallogr F Struct Biol Commun 70(Pt 7): 872-877.

  7. Chen, F., Venugopal, V., Murray, B. and Rudenko, G. (2011). The structure of neurexin 1alpha reveals features promoting a role as synaptic organizer. Structure 19(6): 779-789.

  8. Venugopal, V., Datta, A. K., Bhattacharyya, D., Dasgupta, D. and Banerjee, R. (2009). Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data. Acta Crystallogr D Biol Crystallogr 65(Pt 11): 1187-1195.

  9. Venugopal, V., Sen, B., Datta, A. K. and Banerjee, R. (2007). Structure of cyclophilin from Leishmania donovani at 1.97 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun 63(Pt 2): 60-64.

  10. Sen, B., Venugopal, V., Chakraborty, A., Datta, R., Dolai, S., Banerjee, R. and Datta, A. K. (2007). Amino acid residues of Leishmania donovani cyclophilin key to interaction with its adenosine kinase: biological implications. Biochemistry 46(26): 7832-7843.

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