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Integrated Structural Biology Grenoble at the IBS

Published on 30 April 2020
About ten platforms of the Institute of Structural Biology (IBS) are gathered within the ISBG (Unité Mixte de Service). They offer a catalogue of methods, expertise and instruments for structural biology projects, from protein production, purification and crystallization, to structural characterization, biophysical characterization and sample quality control. Thanks to the support of lean-to research teams, the range of tools offered covers the study of proteins, from gene cloning to the determination of their structure and the understanding of their functioning mechanisms.

Located on the Grenoble European campus, the ISBG platforms benefit from the proximity of major research instruments, such as the neutron sources of the Laue Langevin Institute (ILL) and the facilities of the Grenoble European Synchrotron (ESRF), providing a culture of welcoming visitors and strong technical expertise.

Expertise and services:

Mass Spectrometry (more):
Analysis of intact proteins and macromolecular assemblies,
Determination of the exact mass of high resolution proteins and peptides,
Control of expression, modification, mutation and labelling of proteins and peptides,
Analysis of protein-limited proteolysis and macromolecular complexes by native mass spectrometry.

Electron Microscopy (more):
Negative staining: direct visualization of proteins from 50-100 kDa and quality control,
Cryo electron microscopy, image analysis and tomography: visualization of intact samples, interactions and biological implications,
Cellular electron microscopy: morphological study of cells, bacteria, tissues, protein localization at the subcellular level, monitoring of the virus infection cycle…

Structural Analysis by NMR (more):
Characterisation of the structure and dynamics of molecular complexes,
Development of pharmacologically active molecules,
Characterisation of the degree of protein folding,
Development of liquid and solid NMR methods for complex samples,
Availability of a library of NMR analysis methods,
Adaptation of isotopic labelling protocols for specific proteins or large-scale production.

Structural Analysis by X Ray:
Automated beamline for protein crystallography by diffraction or multiwavelength analysis (more)
UV-visible and Raman spectroscopy on nano-volumic biological samples (more)

Cellular Imaging (more):
Provision of a confocal microscope, a video microscope and a flow cytometer for the study of living cells (counting and visualization),
Image analysis and processing.
Biophysics Characterisation (more):
Measurements of affinity, thermodynamics parameters, by microcalorimetry (ITC),
Characterisation of kinetics of biomacromolecular interactions by surface optical methods (SPR, BLI),
Characterisation of the size, composition, affinity, homogeneity, of macromolecules and complexes (AUC, SEC-MALS),
Quantification of interactions with fluorescent biomacromolecules (MST),
Size determination by light scattering, alone (DLS), or combined (SEC-MALS, NTA),
Development of quality control protocols for specific samples by combining biophysics methods.

Cell Free Expression (more):
Large-scale production (mg) of soluble, membrane and RNA proteins under RNAse free conditions,
Optimization of reaction conditions for large-scale expression: small-scale screening of protein and RNA expression.

Creation of libraries of truncations and punctual mutagenesis, including in co-expression format,
Robotic screening for the identification and optimisation of genetic constructs.

High Throuput Crystallisation (more):
High throughput crystallisation of soluble or membrane proteins in lipidic phase (LCP),
Automated crystallisation of proteins under anaerobic conditions,
Automated visualisation of crystallisation drop images in visible and UV light,
Automated harvesting of crystals grown in drops.

Gene cloning and directed mutagenesis,
Expression and purification test of proteins expressed in E. coli,
Screening of detergents for membrane protein solubilisation and affinity purification.