Structural Biology Platform

Université de Montréal, Montreal, Québec
What the facility does

Structural and biophysical characterization of biomolecular complexes at the atomic scale.

Areas of expertise

The Structural Biology Platform at the Université de Montréal offers access to several state-of-the-art scientific instruments intended to answer structural biological questions for the scientific community. The Platform is comprised of three high field nuclear magnetic resonance (NMR) spectrometers (500 MHz, 600 MHz with cryo-probe and 700 MHz) controlled with NEO consoles from Bruker. A small angle X-ray scattering (SAXS) instrument, with high-throughput robotics is also available. The SAXS can be coupled to a liquid chromatography system for SEC-SAXS applications.

Other instruments for biophysical investigations of biomolecules complement the platform: a size-exclusion chromatography system coupled to a multi-angle light scattering detector (SEC-MALS), an isothermal titration calorimetry (ITC) instrument as well as several liquid handling robots for rapid bio-molecular crystal preparation and screening. Users have also access to a bioinformatics room with several Linux computers for data analysis. Dedicated qualified personnel is always available and will teach and support users on the instruments to maximize the quality of the data acquired at the Platform. Research consultation and turn-key services are also available upon request.

Research services
  • High-field biomolecular nuclear magnetic resonance (NMR)
  • Size-exclusion chromatography coupled to small-angle X-ray scattering (SEC-SAXS)
  • Size-exclusion chromatography coupled to multi-angle light scattering (SEC-MALS)
  • Isothermal titration calorimetry (ITC)
  • Bioinformatics and Linux cluster for data processing
  • Fluorescence and UV/VIS spectrophotometry
  • Complete personnel training and technical support during data acquisition
Sectors of application
  • Agriculture, animal science and food
  • Chemical industries
  • Clean technology
  • Life sciences, pharmaceuticals and medical equipment

Equipment

Function

700 MHz Bruker magnet, Bruker Avance NEO console, 5 mm TXI HCN probe, 5 mm BBI probe

Biological Nuclear Magnetic Resonance (NMR). Great resolution and sensitivity. Ideal for multi-dimensional, triple resonance experiments typically used in structural and dynamics studies of proteins and nucleic acids.

600 MHz Oxford Instruments magnet, Bruker Avance NEO console, 5 mm TCI (cryogenic) HCN probe, 5 mm TXI HCN probe

Biological NMR. Improved sensitivity with cryo-probe usage. Ideal for multi-dimensional, triple resonance experiments typically used in structural and dynamics studies of proteins and nucleic acids.

500 MHz Oxford Instruments magnet, Bruker Avance NEO console, 5 mm TXI HCN probe and 5 mm QXI HCNP probe

Biological NMR. Analysis of small molecules, peptides, and biomolecules of small molecular weight. Biomolecule – small molecule titrations. Rapid assessment of the quality of a biomolecular sample to initiate biophysical studies.

Xenocs/SAXSLAB Bio-Nordic SAXS, Excillum MetalJet D2+ 70 kV X-ray source, Dectris PILATUS3 R 300K detector, ÄKTAmicro chromatography system, high-throughput liquid handling robot

BioSAXS-small-angle X-ray scattering. Analysis of biomolecules (proteins, RNA, DNA) in solution, information regarding to variations in the electronic density of molecular structures in solution (size, shape, density and molecular weight of particles).

Dawn HELEOS II MALS coupled to an ÄKTAmicro chromatography system

Size-exclusion chromatography coupled to multi-angle light scattering (SEC-MALS). Absolute technique for the determination of the molar mass and the average radius of gyration (Rg) of biomolecules in solution following a separation by liquid chromatography.

MicroCal iTC200 system

Isothermal Titration Calorimetry (ITC). In-solution, label free measurement of thermodynamic parameters and binding affinity from biomolecular interactions.

Varian Cary Eclipse Fluorescence Spectrometer

Spectrofluorometer. Fluorescence measurement for structural and kinetic studies. Optional accessory fluorescence anisotropy measurements.