postodoctoral position in structural biology

DAVID DEROSIER derosier at brandeis.edu
Mon Oct 1 10:21:45 EST 2001


Opportunities for Postdoctoral Fellows in Electron Cryomicroscopy and
Structural Biology
Prof. David DeRosier (derosier at brandeis.edu).
Rosenstiel Basic Medical Sciences Research Center
Brandeis University

I have a postdoctoral position to study the structure of large
macromolecular machines. The position is fully funded for at least two
years, and we will pay competitive salaries.  Let me know if you or
someone you know is interested.  Here is a brief description of the
available projects:

The cytoskeleton:
The actin cytoskeleton is a set of cellular machines responsible for
many of the dynamic capabilities of eukaryotic cells.  Actin bundles are
a key elements used to shape cells, generate filopodia, and order the
cell cytoplasm.  The project is aimed at determining the structure of
the actin bundle in the brush border cells, as a model system.  These
bundles are the best characterized and most tractable bundles.  The
approach is two pronged beginning with in vitro studies of the
components (actin, fimbrin and villin) and leading to in vivo studies of
intact bundles.  The tool we use is electron cryomicroscopy and image
analysis.

The bacterial flagellum:
The flagellum is a several machines in one.  It is composed of over a
dozen different proteins, with one set making up the rotary motor,
another the drive train, another a bushing and seal, and another the
flagellar export apparatus.  We determining the structures of these
components using electron cryomicroscopy and image analysis, and we are
correlating structural features with the primary sequences of the
component proteins.

The bacterial signaling complex:
The bacterial cell senses the environment and transmits a signal to the
flagellum.  We are using electron cryomicroscopy and image analysis to
determine the structure of a 1.4 megadalton complex of the cytoplasmic
domain of a chemoreceptor, a kinase, and an adaptor molecule.  The
complex is highly active enzymatically, but has an unusual
stoichiometry, which suggests signal integration from several receptors
into a single kinase.







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