We are seeking to appoint a postdoctoral research associate with expertise in protein chemistry and structural approaches (principally cryoEM and cryoET) to dissect the recently discovered lattice-like organisation of the Gram-negative bacterial outer membrane, focusing primarily on Escherichia coli and Pseudomonas aeruginosa. The post, jointly supervised by Colin Kleanthous and Lindsay Baker in the Department of Biochemistry, is part of a Wellcome Trust Discovery Award involving groups in Oxford, University College London and the Rosalind Franklin Institute.
The ideal candidate should have solved bacterial protein structures by cryoEM (or by X-ray crystallography) and used biochemical and biophysical approaches to dissect function. You should hold, or be close to completion, of a relevant PhD/DPhil in Biochemistry, Molecular Biophysics or a related subject area. You should also have proven experience in working within an interdisciplinary research environment.
The post holder will exploit outer membrane protein labelling methods developed in Oxford for structure determination of purified complexes by single particle cryoEM and of supramolecular outer membrane proteins assemblies within vesicles by cryoET. The post holder will also develop a new cell surface biotinylation method with which to ascertain the near neighbours of specific outer membrane proteins within growing bacteria. This full-time fixed-term post is funded by the Wellcome Trust for up to three years in the first instance. The actual starting salary offered will be based on qualifications and relevant skills acquired and will also be determined by the funding available.
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