<!doctype html public "-//W3C//DTD W3 HTML//EN">
<html><head><style type="text/css"><!--
blockquote, dl, ul, ol, li { padding-top: 0 ; padding-bottom: 0 }
--></style><title>Staff Scientist Position
Available</title></head><body>
<div><b><br></b></div>
<div><b>Staff Scientist Position Available<br>
Laboratory of Cell Biochemistry and Biology<br>
National Institute of Health, USA</b><br>
<b></b></div>
<div>A staff scientist position is available in the laboratory of
Jenny Hinshaw at NIH. The qualified candidate may participate
in ongoing research projects of the Hinshaw laboratory
and/or initiate independent research projects in closely related
fields. The successful candidate should have a Ph.D. with postdoctoral
experience in Cell and Structural biology involving cryo-EM and image
processing. </div>
<div><br></div>
<div>A major focus of our research is calculating 3 dimensional
structures of proteins involved in endocytosis and membrane remodeling
events. We currently have solved the structure of a dynamin mutant in
the constricted and non-constricted states to a resolution of 20 Å.
Dynamin is crucial for endocytosis,<i> synaptic</i> membrane
recycling, membrane trafficking within the cell and more recently has
been associated with filamentous actin. Other dynamin family
members are involved in mitochondria division and morphology (Drp1,
Mgm1), anti-viral activity (Mx, hGBP1), and plant cell wall
formation and thylakoid membrane organization (Phragmoplastin, ADLs).
To determine if a common mechanism exists among this unique set of
proteins, we plan to calculate and compare the 3D structure of dynamin
family members using cryo-electron microscopy, helical reconstruction
and single particle methods. Another interest of the laboratory
is to determine the 3-dimensional structure of the nuclear pore
complex (NPC) in<i> C. Elegans</i>. This project will entail
developing a method of isolating NPCs from<i> C. Elegans</i> and
comparing various NPC mutants using the<i> C. Elegans</i>
well-developed genetic system. The 3D structure of<i>
Xenopus</i> NPC was previously solved by Drs. Hinshaw, Carragher and
Milligan and will be used as a model system for developing the<i> C.
Elegans</i> system. </div>
<div><br></div>
<div><br>
Contact: <b> Jenny E. Hinshaw<br>
<br>
</b>Laboratory of Cell Biochemistry and Biology<x-tab>
</x-tab><x-tab> </x-tab><br>
NIDDK, NIH<x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab></div>
<div>Building 8, Room 419<x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab></div>
<div>8 Center Dr MSC 0851<x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab></div>
<div>Bethesda, MD 20892, USA</div>
<div><br></div>
<div><i>phone</i>: +1 301 594 0842<x-tab> </x-tab></div>
<div><i>fax</i>: +1 301 496 9431</div>
<div><i>e-mail</i>:<u> jennyh@helix.nih.gov</u><x-tab>
</x-tab></div>
<div><x-tab>
</x-tab><x-tab>
</x-tab><x-tab>
</x-tab></div>
<div>http://dynamin.niddk.nih.gov/</div>
<div><br></div>
</body>
</html>