postdoctoral position available

[Dr. Per A. Bullough]

POSTDOCTORAL POSITION IN CRYOEM OF BACTERIAL TOXINS

Krebs Institute

University of Sheffield

The BBSRC-funded post, is available for up to 3 years. The project is to
investigate the function and assembly of a pore-forming toxin in membranes
using cryoEM. The successful candidate will work closely with X-ray
crystallographers and molecular biologists. Experience in electron
microscopy of biological molecules and image analysis is desirable but
training can be provided. The level of appointment is negotiable.

Informal enquiries can be made to Dr. Per A. Bullough
(p.bullough at sheffield.ac.uk, http://www.shef.ac.uk/uni/projects/cryoem)

Application forms and an information pack are available from
jobs at sheffield.ac.uk or +44 114 222 1631 (24 hr.). Please quote reference
RW2403 and give your full postal address.

Closing date for receipt of applications: 13 September 2001

JOB DESCRIPTION

Essential

The successful candidate will be expected to hold a Ph.D. in a relevant
discipline, i.e. Biochemistry, Microbiology, Molecular Biology, Biophysics,
Physics or Chemistry


Advantageous but not essential

Experience of some of the following would be a great advantage but where
necessary, training will be provided.

·	routine protein purification procedures
·	membrane protein reconstitution
·	2-dimensional membrane protein crystallisation
·	negative stain electron microscopy
·	electron cryomicroscopy
·	protein labelling for electron microscopy
·	single particle image analysis
·	2D crystal image analysis


Job description

Our recent structure determination of the E. coli toxin haemolysin E (HlyE)
has revealed the architecture of the solution form of a novel family of
pore-forming toxins, and preliminary electron microscopy studies have given
insights into the arrangement of the transmembrane pores, leading us to
propose a novel mode of protein: membrane interaction  (Wallace et al (2000)
Cell 100: 265-276). This initial structural work has raised further
intriguing questions relating to the function and assembly of this toxin
complex in the membrane, with wide implications for other membrane proteins.
We aim to further probe aspects of the structure of HlyE in solution and in
the membrane pore using a powerful combination of biochemistry, X-ray
crystallography and electron cryo-microscopy (EM). The EM aspects of the
work will involve:

· Determination of low-resolution 3-dimensional structure of membrane-bound
pore complexes by negative stain EM.
· Determination of quarternary structure of pore complexes by
high-resolution cryoEM.
· 2-D crystallization trials of membrane-bound complexes for high-resolution
analysis of the pore structure.
· Identification of labelled sites in HlyE pores using tags such as gold
clusters by EM.

This post is funded through the Biotechnology and Biological Sciences
Research Council for up to 3 years in the first instance. The successful
candidate will join a collaborative project involving applications of cryoEM
in the laboratory of Dr. Per Bullough, X-ray crystallography in the
laboratory of Prof. Peter Artymiuk and molecular biology and protein
biochemistry in the laboratory of Dr. Jeff Green.

-----------------------------------------

Dr. Per A. Bullough
Krebs Institute for Biomolecular Research
Dept. of Molecular Biology and Biotechnology
University of Sheffield
Firth Court
Western Bank
Sheffield S10 2TN
United Kingdom

Tel:      0114 222 4245
Fax:      0114 272 8697
e-mail:   p.bullough at sheffield.ac.uk
          mb1pb at scammonden.shef.ac.uk

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