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

Best
wishes, Matthew Blakeley

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 

 

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 

 

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

 

Description
of the project at ILL

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), 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.