Research

EMBL Grenoble has three principle activities. We collaborate with the ESRF and ILL in developing methods and instrumentation for structure determination by X-ray and neutron crystallography. In our biology labs we do research in molecular structural biology notably in the fields of protein-RNA complexes involved in RNA metabolism and translation; ribosomal assemblies in protein targeting and translocation; protein-DNA complexes involved in transcription; structure, assembly and host-cell interactions of viruses, and proteins involved in membrane fusion. And lastly, we develop instruments and technologies dedicated to automated expression and crystallisation of proteins.

Within this unique environment, EMBL Grenoble has a very active in-house research unit in structural biology making use of a wide range of techniques including molecular biology, biochemistry, electron microscopy, light scattering, neutron scattering, X-ray crystallography and computing. The availability of such a range of techniques is vital to the success of ambitious projects in modern structural molecular biology, and combined with the neighbouring large-scale facilities, provides an ideal environment for the training of young scientists.

There are currently nine research groups. Amongst the research topics being tackled, there is a strong tradition in studying systems involving protein-nucleic acid complexes on the one hand and viruses on the other hand. Structural work on aminoacyl-tRNA synthetases is particularly well known. A number of synthetases were first cloned at EMBL Grenoble and six different synthetase structures have been determined including three in complex with cognate tRNA. Studies on protein-RNA systems include the mammalian signal recognition particle and several proteins which interact with mRNA. This has recently been extended to studies by Cryo-EM of ribosomal complexes involved in co-translational processes.

Another major focus is the study of RNA viruses such as influenza and rabies with the aim of understanding how they replicate and assemble. Protein crystallography of eukaryotic transcription factor-DNA complexes is also another important topic, highlights being the structure determination of the T-protein/DNA complex and the first Stat/DNA complex.

EMBL Grenoble has three principle activities. We collaborate with the ESRF and ILL in developing methods and instrumentation for structure determination by X-ray and neutron crystallography. In our biology labs we do research in molecular structural biology notably in the fields of protein-RNA complexes involved in RNA metabolism and translation; ribosomal assemblies in protein targeting and translocation; protein-DNA complexes involved in transcription; structure, assembly and host-cell interactions of viruses, and proteins involved in membrane fusion. And lastly, we develop instruments and technologies dedicated to automated expression and crystallisation of proteins.

Within this unique environment, EMBL Grenoble has a very active in-house research unit in structural biology making use of a wide range of techniques including molecular biology, biochemistry, electron microscopy, light scattering, neutron scattering, X-ray crystallography and computing. The availability of such a range of techniques is vital to the success of ambitious projects in modern structural molecular biology, and combined with the neighbouring large-scale facilities, provides an ideal environment for the training of young scientists.

There are currently nine research groups. Amongst the research topics being tackled, there is a strong tradition in studying systems involving protein-nucleic acid complexes on the one hand and viruses on the other hand. Structural work on aminoacyl-tRNA synthetases is particularly well known. A number of synthetases were first cloned at EMBL Grenoble and six different synthetase structures have been determined including three in complex with cognate tRNA. Studies on protein-RNA systems include the mammalian signal recognition particle and several proteins which interact with mRNA. This has recently been extended to studies by Cryo-EM of ribosomal complexes involved in co-translational processes.

Another major focus is the study of RNA viruses such as influenza and rabies with the aim of understanding how they replicate and assemble. Protein crystallography of eukaryotic transcription factor-DNA complexes is also another important topic, highlights being the structure determination of the T-protein/DNA complex and the first Stat/DNA complex.