Joint PhD from The University of Melbourne (Australia) and Sorbonne Université (Paris, France): Analysing the conformations of the ATPase p97 using Cryo-Electron Microscopy

The AAA ATPase p97 is a molecular machine that converts energy stored in ATP into conformational changes to segregate proteins in a variety of essential cellular processes, ranging from protein degradation, gene transcription and membrane fusion. Molecular machines or protein complexes, such as p97, exist in multiple conformations and their biological functions are driven by their ability to switch between conformations. Cryo-electron microscopy is a technique that allows studying molecular machines in native conditions and as such it is able to capture the full-range of conformations they adopt.

In this project, you will study the conformational dynamics and determine the conformational landscape of p97 in vitro (purified protein) and in situ (in cells). You will learn how to prepare samples suitable for cryo-EM analysis, collect and analyse single particle and tomography data. You will also contribute to the development of image analysis/computational methods to analyse conformational dynamics of p97. The techniques you will develop are at the leading edge of protein science and are poised to revolutionise our current understanding of the protein world.

This project is ideal for a student with a strong background in biochemistry/biophysics, some programming knowledge and a keen interest in protein science.

The successful candidate will obtain a joint PhD from The University of Melbourne (Australia) and the Sorbonne Université (Paris, France). He/she will spend three (3) years in the group of Isabelle Rouiller at The University of Melbourne and one (1) year in the group of Slavica Jonic at Sorbonne Université. The PhD will be conducted within a program of cooperation between the CNRS (France) and The University of Melbourne.

Main contact for applications: Isabelle Rouiller (

Application Deadline: July 31st, 2021 or until the position is fulfilled

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