![]() |
Gerald StubbsProfessor of Biological SciencesD.Phil., University of Oxford, United Kingdom
e-mail gerald.stubbs@vanderbilt.edu |
X-ray crystallography, fiber diffraction, filamentous plant virus structure, virus-host interactions.
Knowing the detailed three-dimensional structure of biological
macromolecules and assemblies is essential to an understanding
of their functions, including control of their activity. We are
studying the molecular structure of viruses, in particular the
rod-shaped plant viruses, both for their intrinsic interest and
as models for a wide variety of cellular assemblies. We use the
methods of x-ray crystallography and fiber diffraction.
The structure of tobacco mosaic virus has been determined at 2.9 Å resolution. This has enabled us to understand the mechanism of control of assembly of this virus. Through collaborations with molecular geneticists, we are designing and studying mutations of the virus that affect viral assembly, disassembly, transport, and host symptomatology. We are currently studying several viruses related to TMV, a number of unrelated plant viruses, and a variety of other filamentous assemblies. |
|
Selected Publications
Wang, H., Culver, J.N. and Stubbs, G. (1997). Structure of ribgrass mosaic virus at 2.9 Å resolution. Evolution and taxonomy of tobamoviruses. J. Mol. Biol. 269, 769-779. Wang, H., Planchart, A. and Stubbs, G. (1998). Caspar carboxylates: the structural basis of tobamovirus disassembly. Biophys. J. 74, 633-638. Stubbs, G. (1999). Developments in fibre diffraction. Curr. Opin. Struct. Biol. 9, 615-619. Stubbs, G. (1999). The TMV particle structure and initiation of disassembly. Phil. Trans. Roy. Soc. B354, 551-557. Bunick, C., North, A.C.T. and Stubbs, G. (2000). Evaporative microdialysis: an effective improvement in an established method of protein crystallization. Acta Cryst. D56, 1430-1431. Parker, L., Kendall, A., and Stubbs, G. (2002). Surface features of potato virus X from fiber diffraction. Virology 300, 291-295. pdf file |