Ph.D in Biotechnology & Biophysics from Saha Institute of Nuclear Physics, Kolkata, India
ORAU Post-doctoral Research Associate at Oak Ridge National Laboratory, Oak Ridge, TN, USA
-
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.
-
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.
-
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.
-
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.
-
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.
-
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.
-
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.
-
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.
-
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.
-
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.