Plateforme de cristallographie et biophysique

Plateforme de cristallographie

Inauguré le 20 mai 2003 le laboratoire de radiocristallographie, a profondément évolué  pour répondre à de nouvelles attentes.

Depuis 2014, la plateforme offre désormais deux robots de cristallisation de dernière génération pouvant manipuler des phases visqueuses et des solutions de macromolécules biologiques (Mosquito TTP Labtech), deux robots de visualisation de cristaux (4°C et 18°C) ainsi qu’une station de distribution rapide de liquide pour préparer les solutions utilisées par les robots.

La plateforme est principalement utilisée par des utilisateurs autonomes (internes et externes). La plateforme peut fournir un support pour la cristallisation de protéines, notamment pour la cristallisation de protéines membranaires en utilisant des phases cubiques lipidiques.
La plateforme fait partie du réseau Reciprocs d’installations de cristallisation.
Pour résoudre la structure, l’expertise et le soutien peuvent être fournis par le biais d’une collaboration.

Microdépots (50 nanolitres) sur MOSQUITO TTP LABTECH

Contact

Responsable scientifique 

Valérie Biou
CR CNRS – UMR 7099
valerie.biou@ibpc.fr

Ingénieur plateforme 

Franck Brachet
IE CNRS – FR 550
franck.brachet@ibpc.fr

Mail  plateforme cristallographie : cristal@ibpc.fr
Mail plateforme de biophysique :   biophy@ibpc.fr

Station de visualisation EXPLORANOVA

Optimisation sur DRAGONFLY TTP LABTECH

Plateforme de biophysique

La plateforme de biophysique dispose d’un appareil SEC-MALLS installé en 2019 grâce à la mobilité d’un chercheur CNRS au sein de l’IBPC, et d’un microcalorimètre ITC pour la caractérisation thermodynamique des interactions installé en septembre 2023 grâce au CPER PSL RESOLUTION. Les expériences et l’analyse des données sont réalisées par l’ingénieur de la plateforme. L’objectif est d’assurer le contrôle de la qualité des échantillons et leur caractérisation avant l’analyse structurale.

Vue générale du plateau technique

Appareil SEC MALLS , HPLC Shimadzu+UV, diffusion de la lumière Wyatt Treos, réfractomère Wyatt T-reX

Spectrophotomètre de fluorescence VARIAN Cary Eclipse

Remerciements & Tarification

Plateforme de biophysique

Le tarif a été établi à la journée (unité d’oeuvre) selon la décision tarifaire DEC247578DR02.

Nous remercions nos utilisateurs de citer la plateforme pour toute publication utilisant des résultats acquis grâce à la plateforme de biophysique :

The authors acknowledge access to the biophysic platform of the IBPC that is supported by the CNRS, the CPER PSL RESOLUTION.

Tarif à la journée
Clients privés
584.47 €
Clients externes académiques
389.64 €
Clients partenaires
Facturation interne
250.82 €
Coûts éligibles Europe : 250.82 €
Coûts éligibles ANR : 0 €

Nous remercions nos utilisateurs de citer la plateforme pour toute publication utilisant des résultats acquis grâce à la plateforme de biophysique :

The authors acknowledge access to the biophysic platform of the IBPC that is supported by the CNRS, the CPER PSL RESOLUTION.

Plateforme de cristallographie

Le tarif a été établi par plaque de criblage avec ou sans l’assistance de l’ingénieur plateforme (unité d’oeuvre) selon la décision tarifaire DEC247579DR02.

avec l'aide de
l'ingénieur plateforme		 sans l'aide de
l'ingénieur plateforme
Clients privés
541.66 €
311.49 €
Clients externes académiques
361.10 €
207.66 €
Clients partenaires
Facturation interne
207.28 €
Coûts éligibles Europe : 207.28 €
Coûts éligibles ANR : 66.12 €
67.64 €
Coûts éligibles Europe : 67.64 €
Coûts éligibles ANR : 52.90 €

Nous remercions nos utilisateurs de citer la plateforme pour toute publication utilisant des résultats acquis grâce à la plateforme de cristallographie :

The authors acknowledge access to the crystallography platform of the IBPC that is supported by the CNRS, the Labex DYNAMO (ANR-11-LABX-0011)

Label

La plateforme est labellisé IBiSA depuis janvier 2025.

Actualités de la plateforme

Liste de publications

Plateforme de biophysique

5511665 82TPS5CH Biophys_plateforme 1 apa 50 date desc year 2067 http://www.ibpcwp.ibpc.fr/wp-content/plugins/zotpress/
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Saade, C., Pozza, A., Bonnete, F., Finet, S., Lutz-bueno, V., Tully, M. D., Varela, P. F., Lacapere, J.-J., & Combet, S. (2024). Enhanced structure/function of mTSPO translocator in lipid:surfactant mixed micelles. Biochimie. https://doi.org/10.1016/j.biochi.2024.04.008
Mégret-Cavalier, M., Pozza, A., Cece, Q., Bonneté, F., Broutin, I., & Phan, G. (2024). Starting with an Integral Membrane Protein Project for Structural Biology: Production, Purification, Detergent Quantification, and Buffer Optimization—Case Study of the Exporter CntI from Pseudomonas aeruginosa. In L. Journet & E. Cascales (Eds.), Bacterial Secretion Systems : Methods and Protocols (pp. 415–430). Springer US. https://doi.org/10.1007/978-1-0716-3445-5_26
Combet, S., Bonneté, F., Finet, S., Pozza, A., Saade, C., Martel, A., Koutsioubas, A., & Lacapère, J.-J. (2023). Effect of amphiphilic environment on the solution structure of mouse TSPO translocator protein. Biochimie, 205, 61–72. https://doi.org/10.1016/j.biochi.2022.11.014
Abel, S., Marchi, M., Solier, J., Finet, S., Brillet, K., & Bonneté, F. (2021). Structural insights into the membrane receptor ShuA in DDM micelles and in a model of gram-negative bacteria outer membrane as seen by SAXS and MD simulations. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1863(2), 183504. https://doi.org/10.1016/j.bbamem.2020.183504

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Le Moigne, T., Santoni, M., Jomat, L., Lemaire, S. D., Zaffagnini, M., Chéron, N., & Henri, J. (2024). Structure of the Calvin-Benson-Bassham sedoheptulose-1,7-bisphosphatase from the model microalga Chlamydomonas reinhardtii. eLife, 12. https://doi.org/10.7554/eLife.87196.2
Le Moigne, T., Sarti, E., Nourisson, A., Zaffagnini, M., Carbone, A., Lemaire, S. D., & Henri, J. (2022). Crystal structure of chloroplast fructose-1,6-bisphosphate aldolase from the green alga Chlamydomonas reinhardtii. Journal of Structural Biology, 214(3), 107873. https://doi.org/10.1016/j.jsb.2022.107873
Meynier, V., Iannazzo, L., Catala, M., Oerum, S., Braud, E., Atdjian, C., Barraud, P., Fonvielle, M., Tisné, C., & Ethève-Quelquejeu, M. (2022). Synthesis of RNA-cofactor conjugates and structural exploration of RNA recognition by an m6A RNA methyltransferase. Nucleic Acids Research, 50(10), 5793–5806. https://doi.org/10.1093/nar/gkac354
Makamte, S., Thureau, A., Jabrani, A., Paquelin, A., Plessis, A., Sanial, M., Rudenko, O., Oteri, F., Baaden, M., & Biou, V. (2022). A large disordered region confers a wide spanning volume to vertebrate Suppressor of Fused as shown in a trans-species solution study. Journal of Structural Biology, 214(2), 107853. https://doi.org/10.1016/j.jsb.2022.107853
Oerum, S., Catala, M., Bourguet, M., Gilet, L., Barraud, P., Cianférani, S., Condon, C., & Tisné, C. (2021). Structural studies of RNase M5 reveal two-metal-ion supported two-step dsRNA cleavage for 5S rRNA maturation. RNA Biology, 18(11), 1996–2006. https://doi.org/10.1080/15476286.2021.1885896
Le Moigne, T., Gurrieri, L., Crozet, P., Marchand, C. H., Zaffagnini, M., Sparla, F., Lemaire, S. D., & Henri, J. (2021). Crystal structure of chloroplastic thioredoxin z defines a type-specific target recognition. The Plant Journal, 107(2), 434–447. https://doi.org/10.1111/tpj.15300
Le Moigne, T., Crozet, P., Lemaire, S. D., & Henri, J. (2020). High-Resolution Crystal Structure of Chloroplastic Ribose-5-Phosphate Isomerase from Chlamydomonas reinhardtii-An Enzyme Involved in the Photosynthetic Calvin-Benson Cycle. International Journal of Molecular Sciences, 21(20). https://doi.org/10.3390/ijms21207787
Oerum, S., Dendooven, T., Catala, M., Gilet, L., Dégut, C., Trinquier, A., Bourguet, M., Barraud, P., Cianferani, S., Luisi, B. F., Condon, C., & Tisné, C. (2020). Structures of B. subtilis Maturation RNases Captured on 50S Ribosome with Pre-rRNAs. Molecular Cell, 80(2), 227-236.e5. https://doi.org/10.1016/j.molcel.2020.09.008
Oerum, S., Catala, M., Atdjian, C., Brachet, F., Ponchon, L., Barraud, P., Iannazzo, L., Droogmans, L., Braud, E., Ethève-Quelquejeu, M., & Tisné, C. (2019). Bisubstrate analogues as structural tools to investigate m6A methyltransferase active sites. RNA Biology, 16(6), 798–808. https://doi.org/10.1080/15476286.2019.1589360
Lemaire, S. D., Tedesco, D., Crozet, P., Michelet, L., Fermani, S., Zaffagnini, M., & Henri, J. (2018). Crystal Structure of Chloroplastic Thioredoxin f2 from Chlamydomonas reinhardtii Reveals Distinct Surface Properties. Antioxidants, 7(12), 171. https://doi.org/10.3390/antiox7120171