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MXIS - Macromolecular Crystallography, X-ray Imaging & Scattering

Beamlines & support

         Support labs and infrastructure

 

Contacts

2021-09-06_HIGHER EDUC PHD PROGRAMME-4.jpg (HIGHER EDUCATION AND PHD PROGRAMME)   Montserrat Soler Lopez
Head of Group
+33 (0)4 76 88 17 70
 
     
Nanao_Cande.jpg (ID23-2)   Max Nanao
Group Deputy
+33 (0)4 76 88 40 87
 

The Macromolecular X-ray Crystallography, Imaging, and Scattering Group (MXIS) operates a world-leading suite of beamlines and support facilities for studies of biological macromolecules and soft matter. Jointly operated with the EMBL Grenoble, the portfolio includes five macromolecular crystallography (MX) beamlines (ID23-1, ID23-2, ID30-A1, ID30-A3, and ID30B); a serial crystallography beamline (SSX, ID29), two solution scattering beamlines (BM29 and ID02). A cryo-electron microscope (CM01) is jointly operated with EMBL and IBS. Complementary facilities include in-crystallo spectroscopy (icOS), high-pressure-driven crystal cryo-cooling (HPMX). A dedicated biology laboratory (CIBB lab) and biomedical facility (BMF) support sample preparation and cryo-preservation, alongside with biophysical characterisation (PSCM).

Together, this portfolio enables experiments from atomic to mesoscopic length scales, combining high-throughput automated MX with solution scattering (including (U)SAXS/WAXS) and time-resolved approaches to follow structural changes and kinetics from angstrom to micron scales, down to microsecond timescales. Cryo-EM further extends the toolkit through high-resolution single-particle analysis (SPA) and cryo-electron tomography (cryo-ET) for 3D imaging in more native contexts. Integrated onsite support strengthens end-to-end workflows, from sample preparation to experimental readiness across techniques.

Science & Applications

MXIS supports a broad interdisciplinary user community investigating biological macromolecules and their assemblies. Typical application areas include:

  • Structural biology & molecular mechanisms (MX, ID29): High-resolution structures of proteins, nucleic acids, and complexes; challenging microcrystals and radiation-sensitive systems; analysis of conformational dynamics, complex formation, and functional states.
  • Drug discovery (MX): structure-guided ligand discovery and optimisation supported by automated workflows and integrated biophysical characterisation linking binding, stability, and function.
  • Solution scattering (BM29/ID02): Characterisation of molecules and assemblies in solution—oligomerisation, flexibility, and conformational ensembles—often combined with crystallography and complementary biophysics.
  • Cryo-EM and multimodal workflows (CM01): SPA for large/heterogeneous complexes and cryo-ET for 3D imaging in near-native contexts, complementing X-ray approaches.
  • Multiscale scattering for soft matter and hierarchical biology (ID02): (U)SAXS/WAXS to quantify structure and structural evolution from nanometres to microns in polymers, colloids, gels, emulsions, and other soft materials, as well as in biological tissues and biomaterials. Applications link processing or physiological conditions (e.g., flow/shear, temperature, hydration, mechanical load) to ordering, morphology, anisotropy, and structural heterogeneity.

Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.