University of Montreal

Contact Info:

Normand Cyr

Université de Montréal, Pavillon Roger-Gaudry

2900, boul. Édouard-Montpetit, office C-313

Montréal, QC H3T 1J4

https://wiki.umontreal.ca/display/BiologieStructurale/Presentation+of+the+platform

Grants and Identifiers:

RRID: RRID:SCR_022303

CFI30574

Instrumentation:

Other Equipment

Services Provided:

Fluorescence Spectroscopy

Isothermal Titration Calorimetry (ITC)

Mass Photometry

Nuclear Magnetic Resonance (NMR)

Protein NMR

Size Exclusion Chromatography With Multi-Angle Light Scattering

Small Angle X-rays Scattering

Structural Biology

Structure Determination

X-ray Diffraction and Scattering

Relevant Publications:

1.) Gemeinhardt TM, Regy RM, Phan TM, Pal N, Sharma J, Senkovich O, Mendiola AJ, Ledterman HJ, Henrickson A, Lopes D, Kapoor U, Bihani A, Sihou D, Kim YC, Jeruzalmi D, Demeler B, Kim CA, Mittal J, Francis NJ (2025 Feb 26). How a disordered linker in the Polycomb protein Polyhomeotic tunes phase separation and oligomerization bioRxiv, (), 2023.10.26.564264. . PMCID: 10634872.

2.) Ali MG, Wahba HM, Igelmann S, Cyr N, Ferbeyre G, Omichinski JG (2024 Sep). Structural and functional characterization of the role of acetylation on the interactions of the human Atg8-family proteins with the autophagy receptor TP53INP2/DOR. Autophagy, 20(9), 1948-1967. . ID: 38726830.

3.) Petraccione K, Ali MGH, Cyr N, Wahba HM, Stocker T, Akhrymuk M, Akhrymuk I, Panny L, Bracci N, Cafaro R, Sastre D, Silberfarb A, O (2024 Mar). An LIR motif in the Rift Valley fever virus NSs protein is critical for the interaction with LC3 family members and inhibition of autophagy. PLoS pathogens, 20(3), e1012093. . ID: 38512999.

4.) Lemay-St-Denis C, Alejaldre L, Jemouai Z, Lafontaine K, St-Aubin M, Hitache K, Valikhani D, Weerasinghe NW, Létourneau M, Thibodeaux CJ, Doucet N, Baron C, Copp JN, Pelletier JN (2023 Feb 27). A conserved SH3-like fold in diverse putative proteins tetramerizes into an oxidoreductase providing an antimicrobial resistance phenotype. Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 378(1871), 20220040. . ID: 36633286.

5.) Kuttiyatveetil JRA, Soufari H, Dasovich M, Uribe IR, Mirhasan M, Cheng SJ, Leung AKL, Pascal JM (2022 Oct 25). Crystal structures and functional analysis of the ZnF5-WWE1-WWE2 region of PARP13/ZAP define a distinctive mode of engaging poly(ADP-ribose). Cell reports, 41(4), 111529. . ID: 36288691.

6.) Gopinathan Nair A, Rabas N, Lejon S, Homiski C, Osborne MJ, Cyr N, Sverzhinsky A, Melendy T, Pascal JM, Laue ED, Borden KLB, Omichinski JG, Verreault A (2022 Sep 21). Unorthodox PCNA Binding by Chromatin Assembly Factor 1. International journal of molecular sciences, 23(19), . . ID: 36232396.

7.) Lussier-Price M, Wahba HM, Mascle XH, Cappadocia L, Bourdeau V, Gagnon C, Igelmann S, Sakaguchi K, Ferbeyre G, Omichinski JG (2022 Aug 12). Zinc controls PML nuclear body formation through regulation of a paralog specific auto-inhibition in SUMO1. Nucleic acids research, 50(14), 8331-8348. . ID: 35871297.

8.) Dagenais P, Desjardins G, Legault P (2021 Nov 18). An integrative NMR-SAXS approach for structural determination of large RNAs defines the substrate-free state of a trans-cleaving Neurospora Varkud Satellite ribozyme. Nucleic acids research, 49(20), 11959-11973. . ID: 34718697.

9.) Manenda MS, Picard MÈ, Zhang L, Cyr N, Zhu X, Barma J, Pascal JM, Couture M, Zhang C, Shi R (2020 Apr 3). Structural analyses of the Group A flavin-dependent monooxygenase PieE reveal a sliding FAD cofactor conformation bridging OUT and IN conformations. The Journal of biological chemistry, 295(14), 4709-4722. . ID: 32111738.

10.) Lecoq L, Raiola L, Chabot PR, Cyr N, Arseneault G, Legault P, Omichinski JG (2017 May 19). Structural characterization of interactions between transactivation domain 1 of the p65 subunit of NF-κB and transcription regulatory factors. Nucleic acids research, 45(9), 5564-5576. . ID: 28334776.

11.) Cyr N, de la Fuente C, Lecoq L, Guendel I, Chabot PR, Kehn-Hall K, Omichinski JG (2015 May 12). A ΩXaV motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence. Proceedings of the National Academy of Sciences of the United States of America, 112(19), 6021-6. . ID: 25918396.

Description:

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 houses a variety of advanced instruments. It features high-field NMR spectrometers (500, 600, and 700 MHz) with Bruker NEO consoles, ideal for studying protein interactions, RNA-small molecule screening, biomolecular assignments, and structure calculations. The platform also supports biological small-angle X-ray scattering (BioSAXS) with a liquid-metal-jet X-ray source for rapid macromolecular analysis. Additional tools include a TwoMP mass photometer for single-molecule mass measurements, a SEC-MALS system for molar mass determination, an isothermal titration calorimeter (ITC), and robotics for crystal tray preparation. A bioinformatics room equipped with Linux computers is available for data analysis. Highly qualified personnel offer training and support to ensure high-quality data acquisition and analysis. Research consultation and turn-key services are available upon request.