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A
post-doctoral position is available in the “Structural Motility”
Team directed by Dr. Anne Houdusse at the Curie Institute,
Myosins are molecular motors that
convert chemical energy into mechanical energy. The structures for a number of
states for two unconventional motors myosin V and myosin VI have been obtained
in the laboratory. Since myosin V and VI move in opposite direction along actin
filaments, we have also described the structural elements that are essential
for determining the directionality of these molecular motors. Other members of
the family also adopt atypical motility will be the focus of future studies in
the laboratory. Our structural studies on myosin motors have opened the door to
new experiments that directly aim at understanding how force is produced in the
motor and we are looking for a trained crystallographer to perform a number of
structural studies using innovative approaches.
Publications :
Ménétrey, J., et al. 2005. Nature
(London) 435:779-85.
Ménétrey, J., et al. 2007. Cell
131:300-308.
Ménétrey, J., et al. 2008. EMBO J. 27:244-52.
Mukherjea M, et al. Molecular Cell, 5:305-15.
To apply, you must have
a Ph.D. in protein x-ray crystallography; and be highly experienced in protein
crystallization, protein and crystal handling, data collection using
synchrotron and structure determination and refinement. Excellent oral and
written communication skills are a prerequisite.
Interested candidates should send a
CV and three letters of recommandation at Anne Houdusse ([log in to unmask])
http://www.curie.fr/recherche/themes/detail_equipe.cfm/lang/_fr/id_equipe/27.htm
Dr. Anne Houdusse
Group Leader for the Structural Motility team
Directeur de Recherche CNRS - UMR 144 du CNRS
INSTITUT CURIE - Section de recherche
26, rue d'ULM
75248 Paris cedex 05
Tel: 33- 1- 56-24-63-95 Fax: 33- 1- 56-24-63-19
[log in to unmask]