Dear all, please see below for a call for a 3-year full-time research 
fellowship project at the Institut Laue-Langevin in Grenoble, France.


Visualization of hydrogen atoms in carbohydrate-binding proteins and their 
complexes


Context

This 3-year research fellowship is part of the EU Marie Skłodowska-Curie (MSCA) 
COFUND research project AMBER, Advanced Multiscale Biological imaging using 
European Research infrastructures coordinated by the LINXS Institute of 
advanced Neutron and X-ray Science.

AMBER has six core partners: Lund University/MAX IV, Sweden, the European 
Spallation Source (ESS), Sweden, the European Molecular Biology Laboratory 
(EMBL), the Institut Laue-Langevin (ILL), France, the International Institute 
of Molecular Mechanisms and Machines, (IMOL), Poland, and the Leicester 
Institute of Structural and Chemical Biology, UK.


For more information about AMBER: https://www.ambercofund.eu 
[https://www.ambercofund.eu/]


For more information about this Research fellowship (ref 24/58) at Institut 
Laue-Langevin (deadline 24/02/2025) please visit: 
https://www.ill-recruits.eu/generator.php?id=1891 
[https://www.ill-recruits.eu/generator.php?id=1891]


For more information about all the post-doctoral/research fellow positions 
within the AMBER co-fund project: https://www.euraxess.se/jobs/289120 
[https://www.euraxess.se/jobs/289120]


Description of the ILL’s Project

This call is for a 3-year full-time research fellowship project, focused on 
using single-crystal neutron diffraction techniques in combination with other 
structural biology techniques, in order to visualize important hydrogen atoms 
in carbohydrate-binding proteins and their complexes. Protein-carbohydrate 
interactions are involved in the first step of many infectious processes. Many 
pathogens (bacteria, viruses and fungi) recognize sugar epitopes present in 
glycolipids and glycoproteins on host tissue as the first step of infection. On 
the other hand, many human lectins such as the ones of the dendritic cells, 
recognize fragments of bacterial cell wall polysaccharide as the first stage of 
the innate immunity process. A detailed structural knowledge of the 
interactions may serve as the basis for the design of new inhibitors that could 
act as alternative strategies to antibiotic treatment in some infections.

At the Institut Laue-Langevin (ILL) [https://www.ill.eu/], the world’s most 
powerful steady state neutron source, advanced beamlines for neutron 
crystallography are available (LADI and DALI) along with dedicated laboratories 
for the production of fully deuterated proteins (D-Lab). Researchers from the 
Glyco@Alps network at the Institut de Biologie Structurale (IBS) and Centre de 
Recherches sur les Macromolécules Végétales (CERMAV) have expertise in 
production of recombinant human and microbial lectins, respectively. In 
addition, certain saccharides (and their analogs) can be produced in deuterated 
form via a synthetic biology approach, in collaboration with CERMAV (see Gajdos 
et al., 2021, Glycobiology 31, 151; Gajdos et al., Nat. Commun. 13, 194). 
Moreover, the Partnership for Structural Biology (PSB) on the European Photon 
and Neutron (EPN) Science campus provides a unique environment for 
state-of-the-art integrated structural biology with access to many technical 
platforms for sample production, biophysical characterization and structure 
determination.


Name and working place of the Principal investigator

Matthew Blakeley, Large-Scale Structures group, Institut Laue-Langevin, 
Grenoble, France, is responsible for the neutron macromolecular crystallography 
beamlines LADI and DALI. His research uses single-crystal neutron diffraction 
in combination with other structural biology techniques for studies of 
biological macromolecular structure and function, typically health/disease 
related and with a particular focus on structure-based drug design.


Minimum requirements

• PhD in structural biology/chemistry, with excellent knowledge of biochemistry 
and molecular biology, including experience in protein expression, purification 
and crystal growth.

• Applicants need to have a maximum 8 years after a doctoral degree (PhD), as 
required by the Commission, in accordance with the Horizon-Europe MSCA COFUND 
project Grant Agreement.

• At least one original publication in a peer-reviewed journal.

• A complete application package submitted through the AMBER portal (including 
CV and detailed research plan).

• Strict compliance with the MSCA mobility rule that the researcher must not 
have resided or carried out his/her main activity (work, studies, etc.) in the 
host organisation's country for more than twelve months in the three years 
immediately prior to the call deadline.

• Applicants should be fluent in English, have good communication skills and 
should demonstrate their ability to develop and conduct high-quality research, 
both in a team and independently.

• Additional expertise for the position: Experience in neutron and X-ray 
single-crystal diffraction techniques (data collection, data 
reduction/structural refinement) and knowledge of programming languages, such 
as Python, would be desirable.


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