Research Fellow in Structural Biology/cryo-EM

Are you an ambitious researcher looking for your next challenge?

Do you have an established background in Structural Molecular Biology?

Do you want to further your career in one of the UKs leading research intensive Universities?

The 203 kDa b-Barrel Assembly Machinery (BAM) complex of Gram negative bacteria is an integral membrane protein that is required for the folding and insertion of outer membrane proteins (OMPs) and hence is essential for cell viability. Despite this central importance, how BAM folds and inserts the multitude of different OMP sequences that comprise the OM, and how this is able to occur efficiently in the crowded OM in the absence of an obvious source of energy such as ATP or a proton gradient, remain unclear. We are looking for an outstanding postdoctoral research fellow to join an MRC-funded team investigating the mechanism of action of the BAM complex using biochemistry, biophysics and structural biology.

This post will use cryoEM and cryoET, backed up by biochemical and biophysical experiments, to probe the structure and of the BAM complex in different membrane environment and at different stages of its catalytic reaction cycle in OMP folding. Successful execution of this MRC-funded programme grant will thus result in a new molecular understanding of this fascinating complex that is vital for bacterial life.

You will be based in the laboratory of Professors Neil Ranson and Sheena Radford in the Astbury Centre for Structural Molecular Biology at the University of Leeds and will work closely with other members of the membrane protein folding team. You should have a PhD (or be close to completion) in Structural Biology, Biochemistry, Biophysics or a related discipline, with experience of using structural methods for the understanding of protein complexes.