Henning Stahlberg
Adjunct Associate Professor
hstahlberg@ucdavis.edu
Molecular & Cellular Biology
Office
University of California, Briggs Hall 005, Molecular & Cellular Biology, Davis, CA, 95616-8519
(530) 752-8282
Lab
(530) 754 8285
2002
Habilitation
University of Basel, Switzerland
Structural Biology
1997
PhD
EPFL Lausanne, Switzerland
Biophysics
1993
Diploma
Technical University of Berlin, Germany
Physics (Solid State)
The lab studies the structure and function of soluble and membrane proteins by cryo transmission electron microscopy (cryoEM). We employ electron crystallography to study the high-resolution structure of membrane proteins, and use single particle cryoEM and electron tomography to look at the organization and complex formation of proteins at the cellular level. The lab is part of the Center for Structures of Membrane Proteins (CSMP).
http://stahlberglab.ucdavis.edu
NSF CAREER award (2005)
Molecular and Cellular Biology
Also: University Basel, Switzerland
Biophysics
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H. Stahlberg, E. Kutejova, K. Muchova, M. Gregorini, A. Lustig, S. A. Mller, V. Olivieri, A. Engel, A. J. Wilkinson, and I. Barak (2004) Oligomeric structure of the Bacillus subtilis cell division protein DivIVA determined by transmission electron microscopy.
Molecular Microbiology vol 52(5), 1281-1290
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Stahlberg, H., Heymann, B. J., Mitsuoka, K., Fujiyoshi, Y. and Engel, A. (2001) The Aquaporin Superfamily: Structure and Function.
In: Current Topics in Membranes: Aquaporins 51(2), p. 39-119 (Hohmann, S., Agre,
P., Nielsen, S., eds.). Academic Press.
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Stahlberg, H., Müller, D. J., Suda, K., Fotiadis, D., Engel, A., Meier, T., Matthey, U. and Dimroth, P. (2001) Bacterial sodium ATP synthase has an undecameric rotor. EMBO Rep., 2 (3), 229-233.
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Seelert, H., Poetsch, A., Dencher, N., Engel, A., Stahlberg, H. and Müller, D. J. (2000) Proton powered turbine of a plant motor. Nature 405, 418-419.
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Stahlberg, H., Kutejova, E., Suda, K., Wolpensinger, B., Lustig, A., Schatz, G., Engel, A. and Suzuki, C. K. (1999) Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits.
Proc. Natl. Acad. Sci. USA 96 (12), 6787-6790.
Briggs Hall 15
James Evans, lab director; David Carlson, Grad. Student; Po-Lin Chiu, Grad. Student; Hui-Ting Chou, Grad. Student;