Research Fellow in Structural Biology

Leeds, United Kingdom
£33,797 to £40,322 p.a.
05 Mar 2020
02 Apr 2020
Life sciences, Biological Sciences
Fixed Term
Full Time

Are you looking to apply your skills in Structural Biology and Imaging to gain a new molecular understanding of the biogenesis of the outer membrane of Gram-negative bacteria, and help develop new routes to combat bacterial infections?

We are looking for an outstanding postdoctoral research fellow to join our well-established, interdisciplinary team that is investigating how outer membrane proteins are folded by the b-barrel Assembly Machinery (BAM) complex of Gram negative bacteria. BAM 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 structural biology biochemistry, and biophysics.

This post will primarily use structural biology, especially cryoEM and cryoET. The programme will also involve the use of molecular biology, OMP folding assays, fluorescence, FRET, MS cross-linking, and other biochemical/biophysical methods, so there are opportunities to hone a broad range of skills. We aim to:

(1) Determine the structure of BAM and the complexes it makes in detergent, nanodiscs, other membrane mimetic systems using cryoEM.

(2) Determine the structures of BAM and the complexes it makes in proteoliposomes, outer membrane vesicles (OMVs), and native outer membranes, using cryoET and/or sub-tomogram averaging.

(3) Assist in the design and implementation of novel assays with which to monitor the folding of multiple OMPs of different size, using enzymology, fluorescence and FRET methods as appropriate

(4) Investigate the mechanism of action of BAM using biophysics/biochemistry

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 laboratories of Professor Neil Ranson & Professor Sheena Radford, and work closely other members of the OMP team (funded by BBSRC and MRC) who are working on BAM structure and function, OMP folding, and the structure and function of periplasmic chaperones. You will have a PhD (or be close to completion) in Structural Biology, Biochemistry, Imaging or a related discipline. You will also have substantial experience in using cryo-electron microscopy/tomography to determine the 3D structures of protein complexes.

To explore the post further or for any queries you may have, please contact: 

Professor Neil A Ranson, Professor of Structural Molecular Biology 
Tel: +44 (0)113 343 7065, Email:


Professor Sheena RadfordAstbury Professor of Biophysics
Tel: +44 (0)113 343 3170, Email:

Location:  Leeds - Main Campus
Faculty/Service:  Faculty of Biological Sciences
School/Institute:  School of Molecular & Cellular Biology / Astbury Centre for Structural Molecular Biology
Category:  Research
Grade:  Grade 7
Salary:  £33,797 to £40,322 p.a.   Due to funding limitations it is unlikely an appointment will be made above £35,845
Working Time:  37.5 hours per week
Post Type:  Full Time
Contract Type:  Fixed Term (Until 31 October 2022)    
Closing Date:  Thursday 02 April 2020
Reference:  FBSAS1030
Downloads:  Candidate Brief   Additional Information