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Coauthors
Ekaterina Heldwein Department of Molecular Biology and Microbiology, Tufts University School of Medicine, USA
1 protocol

Janna M. Bigalke
  • Department of Molecular Biology and Microbiology, Tufts University School of Medicine, USA
  • 1 Author merit

Education

Ph.D., Chemistry (magna cum laude) Max-Planck-Institute of Molecular Physiology, Technical University of Dortmund, 2011

Current position

Postdoctoral Researcher (DFG Research Fellow) Tufts epartment of Molecular Biology and Microbiology Laboratory of Dr. E. E. Heldwein, University School of Medicine, Boston.

Publications

  1. Bigalke, J. M. and Heldwein, E. E. (2015). Structural basis of membrane budding by the nuclear egress complex of herpesviruses. EMBO J 34(23): 2921-2936.
  2. Bigalke, J. M. and Heldwein, E. E. (2015). The Great (Nuclear) Escape: New Insights into the Role of the Nuclear Egress Complex of Herpesviruses. J Virol 89(18): 9150-9153.
  3. Bigalke, J. M., Heuser, T., Nicastro, D. and Heldwein, E. E. (2014). Membrane deformation and scission by the HSV-1 nuclear egress complex. Nat Commun 5: 4131.
  4. Bigalke, J. M., Dames, S. A., Blankenfeldt, W., Grzesiek, S. and Geyer, M. (2011). Structure and dynamics of a stabilized coiled-coil domain in the P-TEFb regulator Hexim1. J Mol Biol 414(5): 639-653.
  5. Bigalke, J. M., Czudnochowski, N., Vollmuth, F., Vogel-Bachmayr, K., Anand, K. and Geyer, M. (2011). Formation of Tat-TAR containing ribonucleoprotein complexes for biochemical and structural analyses. Methods 53(1): 78-84.
  6. Schonichen, A., Bigalke, J. M., Urbanke, C., Grzesiek, S., Dames, S. A. and Geyer, M. (2010). A flexible bipartite coiled coil structure is required for the interaction of Hexim1 with the P-TEFB subunit cyclin T1. Biochemistry 49(14): 3083-3091.
  7. Tan, J., Verschueren, K. H., Anand, K., Shen, J., Yang, M., Xu, Y., Rao, Z., Bigalke, J., Heisen, B., Mesters, J. R., Chen, K., Shen, X., Jiang, H. and Hilgenfeld, R. (2005). pH-dependent conformational flexibility of the SARS-CoV main proteinase (M(pro)) dimer: molecular dynamics simulations and multiple X-ray structure analyses. J Mol Biol 354(1): 25-40.
1 Protocol published
Expression, Purification and Crystallization of the Herpesvirus Nuclear Egress Complex (NEC)
Authors:  Janna M. Bigalke and Ekaterina E. Heldwein, date: 07/20/2016, view: 2207, Q&A: 0
The protocol describes the production and crystallization of the soluble form of the nuclear egress complex (NEC) from Herpes simplex virus 1 and Pseudorabies virus. The NEC is a heterodimer that consists of conserved proteins UL31 and UL34. NEC ...