CEA
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Domaine : Biologie, biophysique et biochimie
Contrat : CDD
A research position with an initial term of two years is available to work on the structural characterization of protein complexes involved in the assembly and transport of iron-sulfur clusters to a client protein responsible for the biosynthesis of a key metabolic cofactor. This position is based in the Metalloproteins Unit at the Grenoble Institute of Structural Biology (IBS/IRIG), with a desired start date of March 1, 2027.
The researcher fellow will carry out original research on the molecular mechanisms of an unusual iron-sulfur cluster assembly machinery that builds the cofactor directly within its client protein. Using a combination of structural biology, in vitro assays, and spectroscopic techniques, the candidate will capture and characterize the successive intermediates of this process. The work will rely mainly on single-particle cryo-electron microscopy and, where possible, X-ray crystallography, to resolve the molecular interactions involved and follow the stepwise assembly of the FeS cluster within the client protein. The long-term goal is to determine how generalizable this process is, in order to make better use of FeS enzymes in large-scale biotechnological applications.
The researcher researcher will establish protocols to produce protein samples suitable for structural and spectroscopic analyses. They will also perform cryo-EM grid preparation, data processing, structural model refinement, and analysis. When possible, they will also prepare crystals and collect diffraction data.
The ideal candidate holds a Ph.D. and has a solid background in laboratory biochemistry, including protein expression and purification and a genuine interest in metalloproteins and enzymatic mechanisms. Experience working under anaerobic conditions is appreciated. Strong experience in structural biology, particularly in cryo-EM and/or X-ray crystallography, is an asset. Some affinity for computational tools, including an interest in basic programming for processing and analyzing structural data, will be greatly appreciated.
We seek a motivated and open-minded researcher with strong communication skills, who thrives in a collaborative, multidisciplinary team. Prior knowledge of the French research system is not required, but would be a valuable asset for greater autonomy in the role.
The successful candidate will join the Metalloproteins Unit at IBS and will work closely with Dr. Yvain Nicolet. The Metalloproteins Unit has a solid experience in the structural study of metalloproteins and has a set of 6 glove boxes to work “from gene to structure” in the absence of oxygen (https://www.ibs.fr/research/research-groups/metalloproteins-group/).
Before applying, we encourage candidates to contact yvain.nicolet@ibs.fr.
🤝 Why join us? ….
By joining the Grenoble Interdisciplinary Institute, you’ll be part of a dynamic and innovative research environment where you’ll have the opportunity to learn, grow and play a key role within a centre of excellence.
…AND THAT’S NOT ALL!
You may be interested in the benefits that come alongside your main role:
A cutting-edge research ecosystem dedicated to topics of significant societal importance.
Training to enhance your skills and boost your career.
A staff committee offering a wealth of social, cultural and sporting benefits.
Practical benefits: staff canteen/meal vouchers, 85% of transport costs covered, and much more.
An exceptional living environment in Grenoble, nestled in the mountains, offering a unique balance between city life and nature.
🚀 Want to be part of the adventure? Apply now and put your energy to work for research and innovation!
In line with the CEA’s commitments to the integration of people with disabilities, this role is open to everyone. The CEA offers adjustments and/or organisational arrangements to facilitate the inclusion of disabled workers
Ville : Grenoble
Anglais : Courant
Français : Intermédiaire
Pay is not stated in the ad.
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Source: Headcount Labs · original listing ↗
Job data: Headcount Labs, ODbL 1.0. Job descriptions belong to their employers.
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