Instruct — FRISBI — PSB Grenoble Cryo-EM Course on Sample Preparation
We are pleased to announce the eighth hands-on “Instruct — FRISBI — PSB Grenoble Cryo-EM Course on Sample Preparation”, jointly organised by the ESRF, EMBL Grenoble, and the IBS, continuing a series initiated in 2018.
📍 Location: European Photon and Neutron Campus, Grenoble, France
📆 Dates: May 19–22, 2026
📝 Application deadline: April 12, 2026
This 3-day workshop is aimed at PhD students, postdoctoral researchers, staff scientists, and team leaders who are new to the field of single-particle cryo-EM.
The course will cover both theoretical and practical aspects of sample preparation, including iterative grid screening and evaluation for sample optimization. Participants will have access to state-of-the-art instrumentation (2× Glacios, 2× Titan Krios, 4× Vitrobot), as well as a demonstration of cryo-FIB milling (2× Aquilos), providing insight into how single-particle cryo-EM connects to cryo-ET workflows.
There is no registration fee. Meals and accommodation will be provided free of charge; however, participants are responsible for their travel to and from Grenoble.
A maximum of 16 participants will be selected. Participants may bring their own samples for testing, subject to suitability.
Applications are now open. Successful applicants will be notified within one week of the deadline.
Please complete the survey following the link below in order to be considered:
https://workshops.ibs.fr/survey/index.php/614337?lang=en
The workshop announcement is available on the Instruct website and on the IBS website, where further details (including the preliminary programme) will be provided soon. Practical information (venue, travel, site access, accommodation) is currently available on the EPN Campus website.
Contact: cryo-em@ibs.fr
This in-person workshop is co-funded by INSTRUCT and FRISBI (ISBG), with additional support from Thermo Fisher Scientific.
FRISBI/ReNaFoBiS webinar
Date : 15 January 2026, 1:00 PM
Speaker : Aurélie Bertin PCC UMR CNRS 168 (Physique des cellules et cancer), Institut Curie
Tittle: Cryo-tomography : a useful tool to study membrane remodeling proteins using reconstituted systems.
To investigate the details on how proteins can reshape membranes, we have been using reconstituted in vitro bottom-up systems to control key experimental parameters: proteins involved, lipid composition, ionic environment… Cryo-electron tomography describes in three dimensions how membranes are reshaped and give details on the organization of proteins bound to lipids. I will present several examples, involving filamentous proteins, illustrating the methodology. For instance, I will describe findings considering proteins involved in cell division: septins and ESCRTs.
Speaker : Denis Chrétien Université de Rennes, UMR 6290, équipe MiToS
Tittle : C- and D-lattices: The missing link between microtubule structure and dynamic instability?
Microtubules display a unique dynamic behavior called dynamic instability, wherein they alternate stochastically between growing and shrinking states (Mitchison and Kirschner, 1984). Although this behavior is precisely regulated in cells by a plethora of microtubule-associated proteins, it is an intrinsic property of microtubules assembled from purified tubulin, indicating that it is encoded in their structure and assembly mechanisms. In this study, we identify new types of lateral interactions between αβ-heterodimers, which we term C and D, in continuity with the classical A and B lattices described about 50 years ago (Amos and Klug, 1974). These newly identified interactions are much weaker than the A- and B-types, impose a substantial inward rotation on the two protofilaments involved in these interactions, and may form in response to high protofilament skew to release mechanical stress when the microtubule closes into highly skewed configurations. They are abundant at the onset of microtubule self-assembly where large GTP caps assemble, and in the presence of several slowly hydrolysable GTP analogues, suggesting a tight link between the nucleotide state of tubulin and the formation of these lattices.
Please register here https://us06web.zoom.us/webinar/register/WN_mZzRudr2SLuiraRN1FYogA
13ième Ecole de Biologie Structurale Intégrative
Registration for the 13th Integrated Strutural Biology school ReNaFoBis at Oléron, France are open.
Registration for the 13th RéNaFoBiS Oléron workshop, dedicated to Integrative Structural Biology, that will take place on the Oléron island (France), from 05 to 12 June 2026 is open.
The main objective of this workshop is to offer a theoretical and practical training in the different techniques used in integrative structural biology (X-ray diffraction, small angle X-ray scattering, NMR, electron microscopy, sample preparation for structural biology, biophysical methods to study and characterize macromolecular interactions). The goals are to explain and illustrate, to an audience mainly composed of doctoral students and young researchers, the contributions and limitations of each method with a strong emphasis on their complementarity/synergies and future developments.
The official language of the workshop is French but some presentations may be given in English, depending on the overall profile of the students. For practicals, English and French speaking groups may be organised.
For registration and more informations please go at https://ecolebios2026.sciencesconf.org/
As the number of places is limited (28 participants), participants will be selected on the basis of a CV and a letter of motivation. The deadline for applications is March 01, 2026.
Applications will be examined and validated upon deposition and registration will be closed once the maximum number of participants has been reached.
FRISBI/ReNaFoBiS webinar
FRISBI/ReNaFoBis webinar on AI & Structural Biology –November 20th at 01:00 PM Paris
Speaker: Charles Kervrann, Inria Rennes, Institut Curie, France
Tittle: Deep learning and Convolutional Neural Network for Macromolecule detection and Identification in 3D Cryo-Cellular Tomograms.
Speaker 2 : Hugues Nury, IBS Grenoble, France
Tittle: RDL receptor and the application of AI-guided protein design for developing safer insecticides.
Please register here https://us06web.zoom.us/webinar/register/WN_Un9gz1WaQ6eFqJSqAcSXOQ
FRISBI/ReNaFoBis webinar on AI & Structural Biology –November 20th at 01:00 PM Paris
Speaker: Charles Kervrann, Inria Rennes, Institut Curie, France
Tittle: Deep learning and Convolutional Neural Network for Macromolecule detection and Identification in 3D Cryo-Cellular Tomograms.
Speaker 2 : Hugues Nury, IBS Grenoble, France
Tittle: RDL receptor and the application of AI-guided protein design for developing safer insecticides.
Please register here https://us06web.zoom.us/webinar/register/WN_Un9gz1WaQ6eFqJSqAcSXOQ
FRISBI/ReNaFoBis webinar May 15 WG Biophysic
May 15th at 01:00 PM Paris
Speaker: Marc Jamin, IBS, Grenoble, France
Tittle: Deciphering the mechanisms of liquid phase separation induced by rabies virus phosphoprotein
Khadeeja Mubashira, Fella Bouchama, Caroline Mas, Christine Ebel, Sylvain Prevost, Thomas Zemb, and Marc Jamin,
Rabies virus (RABV) generates membrane-less liquid organelles (Negri bodies) in the cytoplasm of its host cell, where genome transcription and replication and nucleocapsid assembly take place, but the mechanisms of their assembly and maturation remain to be explained. An essential component of the viral RNA synthesizing machine, the phosphoprotein (P), acts as a scaffold protein for the assembly of these condensates. This intrinsically disordered protein forms star-shaped dimers with N-terminal negatively charged flexible arms and C-terminal globular domains exhibiting a large dipole moment. Our study shows that in vitro self-association of RABV P drives a complex thermoresponsive phase separation with a lower critical solution temperature. Protein dimers assemble already below the saturation concentration, and condensation is driven by attractive conformation-specific interactions leading to reentrant liquid phase separation over a narrow range of salt concentration. We propose a minimal molecular model in which P can adopt three limit conformational states and the disordered N-terminal arms control the interactions between giant dipoles that is consistent with our observations.
e-mail: marc.jamin@ibs.fr
PLEASE REGISTER HERE:
https://us06web.zoom.us/webinar/register/WN_hx7hikloSpexd40swI_UnQ
FRISBI/ReNaFoBis webinar
Visioconference February, 13 at 01 pm
Speaker: Tobias Madl University of Graz, Austria
Tittle “Decoding the Regulatory Role of Post-Translational Modifications with NMR Spectroscopy”
Post-translational modifications (PTMs) are critical regulators of protein function, enabling dynamic control over processes such as RNA processing, signal transduction, and condensate formation. These modifications often play pivotal roles in physiology and diseases, yet their molecular mechanisms remain elusive in many cases. In this webinar, I will demonstrate how Nuclear Magnetic Resonance (NMR) spectroscopy serves as a powerful tool for unraveling the complex role and interplay of PTMs at the molecular level.
The presentation will begin with an introduction to NMR spectroscopy toolbox to study PTMs, providing a foundation for understanding how this technique is applied in these studies. I will then explore key methodologies for introducing post-translational modifications into proteins for NMR analysis, identifying modification sites, and determining modification kinetics. Additionally, I will highlight how NMR can reveal the intricate interplay between different modifications, particularly in the context of intrinsically disordered proteins.
Using arginine methylation and phosphorylation as examples, I will illustrate how these PTMs modulate biological processes, with specific case studies on their roles in RNA processing, signal transduction, and biomolecular condensate formation. These examples will underscore the critical regulatory functions of PTMs in both physiological and pathological contexts and demonstrate how NMR provides unparalleled insights into their molecular dynamics and interactions.
By the end of the webinar, attendees will gain a deeper appreciation for how NMR spectroscopy enables the study of PTMs, offering valuable perspectives for advancing research in protein biochemistry and understanding diseases associated with dysregulated modifications.
Please register here https://cnrs.zoom.us/meeting/register/O43Q26AcRgOGAO4F96pCYQ