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--></style><title>Postdoc position in Oxford,
UK.</title></head><body>
<div><font face="Arial" size="+1" color="#000000"><b>University of
Oxford<br>
Division of Medical Sciences<br>
Sir William Dunn School of Pathology<br>
<br>
Post-doctoral research scientist in structural biology/ biochemistry/
microbial pathogenesis<br>
Salary £19,460 - £29,128 p.a.</b></font><br>
<font face="Arial" size="+1" color="#000000"><b></b></font></div>
<div><font face="Arial" size="+1" color="#000000">Applications are
invited for the above post,<b> funded for 3 years</b> (to start end
2005/ early 2006) by a grant from the UK Medical Research Council, and
based at Sir William Dunn School of Pathology, Oxford.</font></div>
<div><font face="Arial" size="+1" color="#000000"><br>
Gram-negative bacteria commonly use type III secretion systems (TTSSs
or secretons) to inject proteins directly into the host cell during
infection. How secretons are activated only upon physical contact with
host cells is not understood. The following papers (Blocker et al,
2001, JCB; Blocker et al., 2001, Mol Micro; Cordes et al., 2003, JBC;
Blocker et al., 2003, PNAS) describe the path to our present
scientific questions. We have recently identified needle mutants,
which alter the activity of the secreton. Yet, we find no evidence
that the helical structure of these mutant needles is altered (Kenjale
et al. JBC in press and Cordes et al., JMB in press). This indicates
that the needle is a direct part of host cell sensing mechanism but we
do not yet understand exactly how it works. Therefore, we now wish to
apply biochemical, genetic and EM techniques to study how the needle
components interact with the basal body of the apparatus to see if we
can determine a path for transmission of the activation signal. Our
work will be aided by access to microscope facilities internally and
within at the Wellcome Trust for Human Genetics in Oxford, efforts
from Dr. Susan Lea's laboratory (moving into the Dunn School in early
2006) to solve atomic structures of needle and basal body components
and our sharing of their computer facilities to analyse our EM
data.</font><br>
<font face="Arial" size="+1" color="#000000"></font></div>
<div><font face="Arial" size="+1" color="#000000">Candidates must have
past experience (at the graduate or postdoctoral level) with image
analysis of negative stain and cryoEM micrographs (helical analysis
and/or single particle work). Past experience or an interest in
purification of large protein complexes and molecular biology would be
useful, but is not essential.</font></div>
<div><font face="Arial" size="+1" color="#000000"><br>
Informal enquiries may be addressed to Dr. Ariel Blocker
email:</font><font face="Arial" size="+1" color="#0000FF"><u>
ariel.blocker@path.ox.ac.uk</u></font><font face="Arial" size="+1"
color="#000000">, Webpage:</font><font face="Arial" size="+1"
color="#0000FF"><u>
http://users.path.ox.ac.uk/~ablocker/</u></font><font face="Arial"
size="+1" color="#000000">.<br>
<br>
Applications, together with a C.V. detailing previous employment, and
the names and addresses of three referees, should be sent to the
Administrator, Sir William Dunn School of Pathology, South Parks Rd,
Oxford OX1 3RE, UK (FAX: +44-1865-275-515, email:</font><font
face="Arial" size="+1" color="#0000FF"><u>
administration@path.ox.ac.uk</u></font><font face="Arial" size="+1"
color="#000000">, by<b> 25 November 2005</b>. Please quote
reference<b> AB/05/033</b>.</font><br>
<font face="Arial" size="+1" color="#000000"></font></div>
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</pre></x-sigsep>
<div>Ariel J. Blocker, Ph.D.<br>
Guy G.F. Newton Senior Research Fellow<br>
Sir William Dunn School of Pathology<br>
South Parks Rd.<br>
Oxford OX1 3RE<br>
United Kingdom<br>
Tel lab: +44-1865-285-748<br>
Tel office: +44-1865-275-541<br>
FAX:+44-1865-275-515<br>
Webpage: http://users.path.ox.ac.uk/~ablocker/</div>
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