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.
It consists of three high field nuclear magnetic resonance (NMR) spectrometers (500 MHz, 600 MHz with cryo-probe and 700 MHz) controlled with recent NEO consoles from Bruker. A small angle X-rays 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 bio-molecules 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 bio-informatics room with several Linux computers for data analysis.
A dedicated qualified personnel is always available and will teach and support users on the instruments in order to maximize the quality of the data acquired at the Platform. Research consultation and turn-key services are also available upon request.
Recent publications where the instruments of the platform were used
- Petraccione et al. (2024), "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 Pathog 20:e1012093. PMID: 38512999, DOI: 10.1371/journal.ppat.1012093.
- Lemay-Denis et al. (2023), "A conserved SH3-like fold in diverse putative proteins tetramerizes into an oxidoreductase providing an antimicrobial resistance phenotype". Philos Trans R Soc Lond B Biol Sci 378:20220040. PMID: 36633286; DOI: 10.1098/rstb.2022.0040.
- Lussier-Price et al. (2022), "Zinc controls PML nuclear body formation through regulation of a paralog specific auto-inhibition in SUMO". Nucleic Acids Res 50:8331. PMID: 35871297; DOI: 10.1093/nar/gkac620.
- Kuttiyatveetil et al. (2022), "Crystal structures and functional analysis of the ZnF5-WWE1-WWE2 region of PARP13/ZAP define a new mode of engaging poly(ADP-ribose)". Cell Rep 41:111529. PMID: 36288691; DOI: 10.1016/j.celrep.2022.111529.
- Gopinathan Nair et al. (2022). "Unorthodox PCNA Binding by Chromatin Assembly Factor 1". Int J Mol Sci 23:11099. PMCID: PMC9570017; DOI: 10.3390/ijms231911099.
- Dagenais et al. (2021), "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 Res 49:11959. PMCID: PMC8599749; DOI: 10.1093/nar/gkab963
- Manenda et al. (2020), "Structural analyses of the Group A flavin-dependent monooxygenase PieE reveal a sliding FAD cofactor conformation bridging OUT and IN conformations", J Biol Chem 295:4709. PMCID: PMC7136001; DOI: 10.1074/jbc.RA119.011212
- Matsumoto et al. (2020), "Dynamic DNA-bound PCNA complexes co-ordinate Okazaki fragment synthesis, processing and ligation", J Mol Bio 432:166698. PMCID: PMC8727043; DOI: 10.1016/j.jmb.2020.10.032
Acknowledgement of funding
An acknowledgement of funding sources must appear on all publications resulting from the use of the Structural Biology Platform facilities, whether they are copyrighted or not. The following text should be used:
This work is based upon research conducted at the Structural Biology Platform of the Université de Montréal (RRID:SCR_022303). The Platform was funded and is currently supported by the Canadian Foundation for Innovation award #30574.
If space is limited, this abbreviated text may be used:
The UdeM Structural Biology Platform (RRID:SCR_022303) is supported by the CFI award #30574.
We would appreciate if you can inform us upon the publication of results obtained in part with the instruments of the structural biology platform. This will help us follow the productivity of the platform.