How can we analyze clinical samples using electrons and X-rays? The SHINE theme at LINXS aims to bridge the gap between molecules and therapy by making use of electrons and X-rays.
Join us for the theme kick-off on 23 February 2026!
When: 23 February, 2026
Where: at LINXS (LINXS, The Loop, Rydbergs torg 4, Lund), workshop room on the 3 floor.
About
The aim of the theme is to increase the knowledge in the analyses of clinical samples by electron microscopes and combine that with X-rays. Comprehensive understanding of human health and disease requires structural insight at all scales – from atomic to tissue – spanning well beyond the classical definition of structural biology. This theme aims to bridge the scientific gaps between molecular research and translational applications, addressing the most fundamental questions of life, health and disease. The clinical conditions we will specifically focus on are relate to metabolic diseases, neurodegeneration, airway diseases, as well as transmittable diseases caused by viral and bacterial infections.
-
11:45-12:30 Lunch at LINXS
12:45-13:00 Welcome and introduction by Karin Lindkvist
13:00-13:45 WG Metabolic diseases- Isabella Artner
“Resolving Arp2/3 complex-mediated branch nucleation in space and time using cryo-electron tomography”, Marion Jasnin, Helmholtz Munich13:45-14:30 WG Airway and neurodegenerative diseases- Lena Uller and Tomas Deierborg
Speaker: Bryan Falcones, MAXIV and Lund University, “Title”14:30-15:00 Coffee break
15:00-16:30 WG Transmittable diseases- Vasili Hauryliuk
“5:2 molecular motors: from bacterial motility to anti-phage defense”, Nicholas Taylor, Copenhagen University
“SHINE-ing electrons on the replication of arthropod-borne viruses”, Lars-Anders Carlson, Umeå University16:30-16:45 Break
16:45-17:05 cryo-EM and cryo-ET on tissue (Anu Tyagi, Mathieu Coincon)
17:05-17:15 SAXS cross-validation (Christopher Söderberg)
17:15-18:15 Discussions
18:45 Optional buffet at LINXS
-
Resolving Arp2/3 complex-mediated branch nucleation in space and time using cryo-electron tomography
Marion Jasnin, Helmholtz Munich
In this talk, I will demonstrate the potential of cryo-electron tomography (cryo-ET) for time-resolved in situ structural biology research. To illustrate this, I will use our ongoing study of native actin assemblies. Actin plays a pivotal role in numerous cellular processes by forming and disassembling highly dynamic, ordered structures. Nevertheless, our understanding of how the molecular components of the actin machinery collaborate within cells to produce nanonewton force-generating actin systems, such as podosomes in human macrophages or those involved in endocytosis in yeast, remains limited.
I will demonstrate how cryo-ET can be employed to reveal the polarity of actin filaments at the monomer level within podosomes in human macrophages. This approach provides valuable insights into podosome assembly dynamics. It can also be used to recreate the spatial and temporal distribution of Arp2/3 complex-mediated branch junctions in both human macrophage podosomes and in yeast during clathrin-mediated endocytosis. To achieve this, we analyzed the spatial orientation of branch junctions in our cellular tomograms using high-resolution template matching and subtomogram averaging. Based on this information, we simulated successive generations of actin filament branches. We validated our model predictions by comparing the generations assigned by our model with those visualized in our data.
Finally, I will introduce CryoAll: a Vision Transformer model trained on cryo-ET data that can segment various cellular structures, including cytoskeletal elements. Classical methods would fail to do this due to the density and complexity of these actin networks. Our integrative approach therefore reveals the assembly mechanisms of native actin networks at the molecular level, helping us to understand the underlying force generation mechanisms. Proposing time-resolved in situ cryo-electron tomography, this work opens up new avenues in the field of 4D structural biology.
5:2 molecular motors: from bacterial motility to anti-phage defense
Nicholas Taylor, Copenhagen University
Bacteria move through the rotation of large filaments know as flagella. Flagellar rotary motion is powered by a flagellar motor, driven by stator units (MotAB). The MotAB proteins convert the ion motive force across the bacterial inner membrane into rotation of the filament, but it was not understood how this occurred.
Using cryo-EM we have determined structures of the MotAB complex, which we show has a 5:2 stoichiometry shared across different species. By visualizing MotAB in its plugged, inactive state, as well as mimics of its active state, we come up with models for how torque is generated in the flagellar motors, as well as how direction switching in the flagellar motor occurs. We also reveal our recent progress on how ion specificity is obtained and propose a mechanism for how stator units become active upon motor incorporation.
I will also present results on a newly discovered bacteriophage defense system, Zorya, that uses a 5:2 motor complex to sense bacteriophage infection. Using a combination of structural biology, functional assays, light microscopy and mass spectrometry, we provide novel insight into the unique Zorya mechanism of action. We provide data indicating that Zorya detects phage infection by monitoring integrity of the peptidoglycan layer. Upon phage infection, the ZorAB motor proteins get activated and through a 700 Å long tail locally recruit and activate ZorD nuclease that can degrade the phage genome, halting the infection.
SHINE-ing electrons on the replication of arthropod-borne viruses
Lars-Anders Carlson, Umeå University
Many arthropod-borne pathogens are positive-sense RNA viruses. Such viruses replicate their RNA on remodelled cytoplasmic membranes, in membrane-bound viral replication organelles. These replication organelles frequently take the shape of a 50-100 nm, stable membrane bud housing viral enzymes and template RNA. Here, we present our cryo-electron tomography studies of replication organelles from two arthropod-borne virus types - alphaviruses and flaviviruses - with a focus on their macromolecular architecture and biophysical principles of their biogenesis. Alphaviruses, which hijack the plasma membrane to generate replication organelles, gather all the enzymatic activities necessary for genome replication in a 2 MDa protein complex located at the membrane bud neck. This complex further serves to constrain the bud neck, and the membrane budding then relies on the pressure generated from dsRNA polymerisation. This is thus a unique case of polymerase-mediated membrane remodelling. Flaviviruses generate replication organelles on a remodelled ER membrane using very different proteins from alphaviruses. They remodel the replication organelle membrane by a mechanism that relies both on a membrane coat, and on intraluminal pressure from viral dsRNA. In addition, we discuss the close coupling between flavivirus genome replication, virion budding and virion maturation.
Genral questions?
For practical questions about LINXS and the venue, please contact josefin.martell@linxs.lu.se
Please note that if you register for physical participation and do not attend without informing us, a no-show fee of 200 SEK will be charged to offset the cost of ordered food/refreshments etc.
If you don’t receive a registration confirmation please check your spam mail.
During our events we sometimes take photographs and short film clips to profile our activities. Please let us know if you don’t want to be in any photos/films before we start the event. Some webinars are recorded to be used for educational purposes in the LINXS website.
By registering to our events you give your permission to LINXS, according to the General Data Protection Regulation (GDPR), to register your name and e-mail address to be used for the sole purpose of distributing newsletters and communications on LINXS activities.