Postdoctoral Fellow – Structure and dynamics of transcription condensate assembly

Postdoctoral Fellow – Structure and dynamics of transcription condensate assembly

As part of the 3-year DFG-funded Priority Program “Molecular mechanisms of functional phase separation” (https://www.spp2191.com/) the Duss and Mahamid groups are looking to recruit a highly motivated and cross-disciplinary postdoctoral researcher to study mechanisms of bacterial ribosomal RNA transcription condensates by combining biochemistry, single-molecule fluorescence microscopy, and cryo-electron tomography.

The Duss group (https://www.embl.org/groups/duss/) uses single-molecule fluorescence microscopy in combination with integrative structural biological and biochemical approaches to understand how protein-RNA complexes are assembled and work as macromolecular machines, providing new opportunities to fight diseases and to create new functional molecular assemblies. The Mahamid group (https://www.embl.org/groups/mahamid/) pioneers technology development in cryo-electron tomography to study molecular machines in their native functional context and elucidate the in vitro and in situ architectures of functional biomolecular condensates.

Your role

The successful candidate will lead a cutting-edge experimental research project to image both the dynamics and structure of reconstituted bacterial transcription condensates using a multidisciplinary approach in a close collaboration between the Duss and Mahamid labs.

You will develop biochemical assays to understand how phase separation and rRNA transcription efficiency are linked, establish multi-color single-molecule fluorescence microscopy experiments to track in real-time how rRNA transcription condensates are formed, and develop a method for direct correlation with cryo-electron tomography to simultaneously visualize structure and dynamics that are evolving during condensate formation.

You have

• a PhD in structural biology, biophysics, biochemistry, molecular biology or related disciplines (or you are close of finishing your PhD)
• experience in single-molecule fluorescence microscopy and/or biochemistry (optimally in protein expression & purification and in performing RNA or protein-RNA biochemical assays)
• the ability to work independently and creatively
• high commitment and motivation

You might also have

• experience in the field of phase separation
• experience in cryo-electron tomography/ microscopy
• experience in programming (e.g. Python, Matlab)

Why join us

EMBL is an inclusive, equal opportunity employer offering attractive conditions and benefits appropriate to an international research organisation with a very collegial and family friendly working environment. The remuneration package comprises a competitive salary, a comprehensive pension scheme, medical, educational and other social benefits, as well as financial support for relocation and installation, including your family and the availability of an excellent child care facility on campus.

What else you need to know

We are Europe’s flagship research laboratory for the life sciences – an intergovernmental organisation performing scientific research in disciplines including molecular biology, physics, chemistry and computer science. We are an international, innovative and interdisciplinary laboratory with more than 1600 employees from many nations, operating across six sites, in Heidelberg (HQ), Barcelona, Hinxton near Cambridge, Hamburg, Grenoble and Rome. Our mission is to offer vital services in training scientists, students and visitors at all levels; to develop new instruments and methods in the life sciences and actively engage in technology transfer activities, and to integrate European life science research. Please note that appointments on fixed term contracts can be renewed, depending on circumstances at the time of the review.

EMBL is a signatory of DORA. Find out how we implement best practices in research assessment in our recruitment processes here.

Please apply online through: www.embl.org/jobs

Reference Number: HD02262