Nozomi Ando is a Professor in the Department of Chemistry and Chemical Biology at Cornell University. She received her Ph.D. in Physics from Cornell University, followed by an NIH Pathway to Independence Postdoctoral Fellowship at MIT. She began her independent career in 2014 in the Department of Chemistry at Princeton University and moved to Cornell in 2018. Nozomi is an active member of the structural biology community and currently serves as co-PI of the MacCHESS facility at the Cornell High Energy Synchrotron Source (CHESS) and the NE-CAT facility at the Advanced Photon Source (APS). She is also the Director of Graduate Studies in Cornell Chemistry and an advocate for interdisciplinary training and diversity in science. Nozomi's research lies at the interface of physics, chemistry, and biology, with a long-standing focus on developing and applying advanced methods in structural biology. Her lab is particularly known for innovating techniques in X-ray scattering to investigate protein conformational dynamics. She has contributed broadly to the understanding of enzyme regulation and evolution through the integrated use of X-ray scattering, cryo-electron microscopy, and bioinformatics.

Professor Barran holds a Chair of Mass Spectrometry in the Department of Chemistry and is the Director of the Michael Barber Centre for Collaborative Mass Spectrometry and a member of Manchester Institute of Biotechnology, The University of Manchester, UK. She is the deputy chair of the Infrastructure and Capital Advisory Group for the Medical Research Council, UK. Her research interests include: Biological mass spectrometry; Instrument and technique development; Protein structure and interactions; Dynamic and Disordered Systems; Multiomics and Parkinson’s disease Diagnostics. She likes to do things with mass spectrometry that can’t be done with other methods. She is a Fellow of the Royal Society of Chemistry and was awarded the Theophilus Redwood Award from the RSC in 2019, Researcher of the Year 2020 from the University of Manchester and the ACS Measurement Science Lectureship 2021. In 2020 she initiated the COVID-19 Mass Spectrometry Coalition and was appointed as Chief Advisor to the UK Government on Mass Spectrometry as part of their pandemic response. Perdita has had the privilege to mentor 42 graduate students through the successful completion of their PhD’s. as well as 18 postdoctoral fellows. Of the PhD students 22 are female and 20 are male and 39 are still working in STEM, many of who in mass spectrometry, which means she gets to hear about their brilliant contributions to science and society frequently.

Emma Beale is a structural biologist working at the Paul Scherrer Institute in Switzerland. She is based at the Alvra Endstation of the Swiss X-ray Free Electron Laser (SwissFEL) where she supports the ultrafast photochemistry and photobiology experiments carried out there. She develops sample delivery methods for time-resolved protein crystallography with the aim of enabling experiments that measure how proteins move on an atomic scale as they carry out their unique functions. Emma completed an undergraduate degree in Biochemistry at the University of Otago, New Zealand. During her studies, she became fascinated with X-ray crystallography and protein structure and so went on to complete a DPhil in Structural Biology at the University of Oxford. Here, she worked with Prof. Nicole Zitzmann and Dr. Max Crispin on the structural and functional characterisation of immunomodulatory enzymes produced by bacteria. After her studies, Emma moved into the field of methods development for X-ray protein crystallography with a focus on sample preparation and sample delivery. Her research covered methods that make use of very small protein crystals measuring a few microns down to hundreds of nanometers in size. Specifically, whilst at Diamond Light Source Ltd. as a post-doctoral researcher she explored electron diffraction of protein crystals and developed sample preparation and delivery methods for the VMXm beamline. In 2021, she moved to Switzerland to carry out post-doctoral research at SwissFEL and since 2023 has had a permanent position there as part of the Alvra Group supporting experiments and developing infrastructure at the Alvra Endstation.

Tom graduated with a Master’s Degree in Biochemistry from University of Bath in 2003. During this time he discovered a passion for structural biology whilst on a 6 month placement at the ESRF in Grenoble, France. Following this he gained a PhD in Biophysics from the University of Leeds centred on developing new tools for observing protein dynamics using biomolecular NMR. Wanting to focus on computational methods in 2008 he moved to Utrecht in the Netherlands to PostDoc in the group of Piet Gros and developed phenix.ensemble_refinement, combining x-ray structure refinement with molecular dynamics simulations to reveal protein dynamics from crystallography. In 2013 he joined the CCP-EM Core Team and the Science and Technology Facilities Council at the Rutherford Appleton national Laboratory. He is now the Group Leader of Molecular and Cellular Electron Microscopy group in the Scientific Computing department and leader of the CCP-EM Core Team. He works with a team of internal and external software developers to make the CCP-EM software suite – a set of tools for processing biomolecular cryoEM data and producing high resolution maps of proteins used by both academic- and industry-based researchers. Out of the lab he is normally found chasing after his kids or escaping on his bike.

Bridget Carragher received her Ph.D. in Biophysics from the University of Chicago in 1987. She worked in a variety of positions, both in industry and academia before moving to the New York Structural Biology Center in 2015 to lead the Simons Electron Microscopy Center (SEMC), together with Clint Potter. While at SEMC, Bridget and Clint directed the National Resource for Automated Molecular Microscopy (NRAMM), the National Center for CryoEM Access and Training (NCCAT), the National Center for In-situ Tomographic Ultramicroscopy (NCITU), and the Simons Machine Learning Center (SMLC). They also founded the company NanoImaging Services in 2007. Bridget moved to her current role as Founding Technical Director of the Chan Zuckerberg Imaging Institute (CZII) in January 2023. The mission of CZII is to enable deep insights into the architecture of complex biological systems, at the molecular level, through the development and application of novel imaging technologies. The initial grand challenge is to develop technologies and methodologies to image the molecular architecture of the cell to near atomic resolution using cryo electron tomography.

Ashwin Chari completed his undergraduate degree at the ETH Zurich in biochemistry and molecular biology in 2004. He received his PhD, summa cum laude, from the Institute of Biochemistry, University of Würzburg, Germany in 2009. His PhD supervisor was Prof. Utz Fischer, the title of his PhD thesis “The Reaction Mechanism of Cellular U snRNP Assembly”. After a short postdoctoral stay at the University of Würzburg, he moved to the Max Planck Institute for Biophysical Chemistry, Göttingen, Germany in 2011 as DFG-funded Independent Project Leader in the Research Group for 3D Cryo-electron microscopy. He was promoted to Project Leader in the Department of Structural Dynamics in 2016. He is currently a tenured Research Group Leader for Structural Biochemistry and Mechanisms at the Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany. Chari is an author of more 44 research contributions, with > 5000 citations, and an H-index of 34. Chari´s research and scientific area of expertise lies in the mechanistic biochemistry of large macromolecular complexes involved in cellular RNA metabolism, proteostasis and fatty acid synthesis. For this, he and his research group determine high-resolution structures determination of large macromolecular assemblies by X-ray crystallography and cryo-EM, elucidate the inhibition mechanisms of large macromolecular assemblies to aid in drug discovery efforts, and both develop and apply methods for ultra-high resolution Structural Enzymology to decipher reaction mechanisms directly by X-ray crystallographic structures. This most recently is extended towards the application of quantum crystallographic methods to ultra-high resolution structures of enzymes in various reaction states determined by his group.

Anchi Cheng completed her undergraduate degree in Chemistry at National Taiwan University and then her Ph.D at The Ohio State University in USA studying phase transition mechanism using time-resolved X-ray diffraction. She became involved in CryoEM field during her postdoc years at The Scripps Research Institute through the study of structures of aquaporin 1 and cardiac gap junction in the form of two-dimensional crystals. She became a staff scientist at Scripps and focused on automation of CryoEM data acquisition and processing as a part of National Resource for Automated Molecular Microscopy (NRAMM) under the directorship of Bridget Carragher and Clint Potter. She moved to New York Structural Biology Center in 2015 with the two directors. She became a technology team leader in 2023 at Chan Zuckerberg Imaging Institute which has a mission to accelerate cellular cryo electron tomography (cryoET). She is a developer for Leginon, an automated data acquisition and preprocessing software for CryoEM and CryoET.

Paulina Dominiak completed her Master in Science with honors in Chemistry (2000) and Biology (2001) at the University of Warsaw. She received her Ph.D. degree in Chemistry in 2005, with honors, from the University of Warsaw. Her supervisor was Prof. Krzysztof Wozniak. Her thesis was dedicated to weak interactions in organic and protein crystals studied with X-ray crystallography, including experimental charge density analysis. During her studies she visited twice NASA Space Flight Center in Huntsville, Alabama, in the US, to work with dr Ewa Ciszak. She did her postdoctoral research under prof. Philip Coppens supervision, at the University at Buffalo, SUNY, in the US. She spent there two years (2005-2006), working firstly on time-resolved crystallography and then in the charge density field, developing a data bank of atomic electron densities, later on, called the University at Buffalo Databank (UBDB). In 2007 she moved back to the University of Warsaw, Chemistry Department, where she got an Assistant Professor position. Here she was further developing the UBDB and working on its applications to X-ray crystallography and structural biology. For that work, she received a habilitation degree in Chemical Sciences in 2013. In 2017 she got the permanent Associate Professor position and three years later, in 2020 she received the Professor title and Full Professor position.
Paulina is leading the Electron Density Modelling Group at the Biological and Chemical Research Center of the University of Warsaw. Her research is focused on quantum crystallography. Her group is developing new electron density modeling methods applicable to X-ray and electron crystallography, structural chemistry, and molecular biology. Her group is developing the MATTS data bank (successor of UBDB) to be used in TAAM refinements and evaluation of electrostatic properties and interaction energies in molecular crystals and protein-ligand complexes. Currently, she concentrates on the introduction of more accurate electron scattering factors to electron crystallography.
Paulina published more than 80 original research papers with an H-index of 28 and >2400 citations. In 2020 she was elected the chair of the IUCr Commission on Quantum Crystallography. She is also elected member of the Committee on Crystallography, Polish Academy of Sciences and one of the co-editors of Acta Cryst. A.

Radoslav I. Enchev is a structural biologist and Group Leader heading the Visual Biochemistry Laboratory at The Francis Crick Institute in London. Born and raised in Sofia, Bulgaria, he studied molecular biotechnology in Heidelberg before earning his PhD and establishing his own research lab at the Crick, where he leads method development in time resolved cryo EM. His team builds microfluidic platforms to capture biochemical reactions with millisecond resolution—essentially creating molecular “movies” of processes such as enzyme catalysis and SCF ubiquitin ligase dynamics. His research also includes foundational work using modular microfluidics to enable kinetic insight from time resolved cryo EM. His contributions bridge structural biology and dynamic molecular visualization, advancing our understanding of cellular regulation at atomic and temporal precision.

Philipp S. Erdmann is a Chemical and Structural Biologist specializing in cryo-Electron Tomography (cryo-ET). Born in Würzburg, Germany, he studied Organic Chemistry at the Julius Maximilian University of Würzburg before earning his PhD from the Ludwig Maximilian University of Munich, where he pioneered chemical optogenetics approaches to control endogenous ionotropic glutamate receptors with light. As a postdoctoral fellow at MIT, he developed advanced imaging techniques for synaptic proteins, followed by a position at the Max Planck Institute of Biochemistry under Jürgen Plitzko and Wolfgang Baumeister. There, he led a Structural Biology project group, applying 3D correlative FIB milling to study autophagic structures and ribosome biogenesis. Currently, as a Research Group Leader at Human Technopole (Milan, Italy), Philipp focuses on subcellular protein localization and innovative cryo-EM techniques, including cryo-FIB milling, cryo-lift-out, and expansion microscopy. His work addresses fundamental biological questions, particularly phase separation in neurodegenerative diseases.

Andrea Graziadei is a structural biologist and structural bioinformatician specializing in integrative modelling and crosslinking mass spectrometry. He obtained his PhD from EMBL with a thesis focussed on NMR and small-angle scattering in the lab of Dr. Teresa Carlomagno. He then moved on to the lab of Prof. Juri Rappsilber in at the Technische Universitaet Berlin, where he helped develop strategies for integrative modeling with crosslinking mass spectrometry, cryo-electron microscopy data and deep learning. His work focussed on ribosome biogenesis and transcription-translation coupling. Since 2022, he manages the structural proteomics unit at Human Technopole in Milan, which focusses on providing crosslinking mass spectrometry and other advanced proteomics techniques to the Italian scientific community. As part of his work in Milan, he has helped with validating the conformation of ciliary transport trains and POLIII initiation complexes at snRNA promoters.

Prof Pippa Hawes is Deputy Lead of the EM Science Technology Platform (STP) at the Francis Crick Institute in London. The facility specialises in volume correlative imaging of cells and tissues, applied to projects covering the Institute’s remit of Biomedical research aimed at improving treatment, diagnosis and prevention of human disease. Pippa completed a MSc degree in Biological Electron Microscopy before taking a technical post at The Pirbright Institute, a veterinary virology research institute in the UK, where she completed her PhD in-post. She recently moved to the Crick after >20 years studying viral infection of cells using light and electron microscopy, leading the Bioimaging facility at Pirbright for the last 12 years. Pippa also held an honorary scientist position at the electron Bioimaging Centre (eBIC) at Diamond Light Source Ltd (2019 – 2023) where she was involved with projects studying viral infection in cells using in situ structural biology (cryo-FIBSEM/cryo-ET). She strongly believes that volume electron microscopy and in situ structural biology are complementary techniques that should be utilised together more often in research.

Grant Jensen earned his PhD from Stanford University, where he studied electron microscopy of RNA polymerase and other protein complexes under Dr. Roger Kornberg, a Nobel prize winner. Jensen continued his work in protein electron microscopy as a Damon Runyon-Walter Winchell post-doctoral fellow under the supervision of Dr. Kenneth Downing at the Lawrence Berkeley National Lab, where he expanded his interests to include electron tomography of whole cells. He spent 18 years as a professor of biology and Biophysics at Caltech, where his research focused on the ultrastructure of small cells, the structural biology of HIV, and the further development of cryo-EM technology. He left Caltech in 2020 to become Dean of Brigham Young University’s College of Computational, Mathematical, and Physical Sciences, where he oversees seven departments in addition to maintaining his own lab. Together with his colleagues, Grant has published nearly 200 papers. He’s passionate about creating accessible sources for people to learn about cryo-EM, which is why he’s created a free online textbook, The Atlas of Bacterial and Archaeal Cell Structure, which is full of stunning tomograms and basic biology, and a free online course, Getting Started in Cryo-EM, which teaches the fundamentals of cryogenic electron microscopy.

Eaazhisai Kandiah (Isai) is a structural biologist with a strong interest in virus structure and function. With a background in Physics, she completed her PhD at the Indian Institute of Science in Bangalore in 2004, studying enzymes from the malaria parasite Plasmodium falciparum using X-ray crystallography. Following her PhD, she held postdoctoral positions at ETH Zurich, the National Institutes of Health (USA), EMBL Grenoble, and the Institut de Biologie Structurale. During this time, she applied integrated structural biology approaches, mainly cryo-electron microscopy (cryo-EM) and X-ray crystallography, to investigate a wide range of biological systems, including viral assembly, transcription regulation, and bacterial stress responses. In 2017, Isai joined the European Synchrotron Radiation Facility (ESRF) in Grenoble, where she is now the principal beamline scientist for the CM01 cryo-EM facility. Her current work focuses on understanding how beta-coronaviruses, particularly SARS-CoV-2, replicate, using both single-particle analysis and cryo-electron tomography. She also involves in methodological developments in cryo-EM.

Nikolai Klena received his B.S. with Distinction honors in Biology (2012) at Juniata College in the United States. He then spent 4 years as a technician at the University of Pittsburgh, where he contributed to uncovering a central role for cilia in the pathogenesis of congenital heart disease. Klena received his PhD from the University of Geneva in Switzerland (2021), utilizing cryo-electron tomography (cryo-ET) to examine the structural conservation of centrioles and basal bodies, as well as helping develop new expansion microscopy (ExM) methods. Moving to Human Technopole in Milan, Italy (2021) as a postdoctoral fellow, Klena combined cryo-ET and volume electron microscopy with ExM to better understand ciliary ultrastructure. He is particularly focused on integrating ExM with other structural techniques. Such as developing direct correlation pipelines, as well as more building integrative structural models of biological systems.

Abhay Kotecha is a structural biologist specializing in cryo-electron microscopy (cryo-EM) and cryo-electron tomography (cryo-ET). He currently serves as Senior Director of Technologies for Cryo-EM and Cryo-ET at St. Jude Children's Research Hospital, where he leads the implementation of the newly formed Center of Excellence for Structural Cell Biology (CoE-SCB), with a mission to bridge multiscale imaging from tissues to atoms using cryo-ET, volume EM, and automation technologies. Dr. Kotecha earned his DPhil in Structural Biology from the University of Oxford and holds a BSc in Cell and Molecular Biology from Oxford Brookes University. Prior to joining St. Jude, he was a group leader at Thermo Fisher Scientific, where he contributed to advancing high-throughput and high-resolution cryo-EM imaging technologies. His expertise includes structure-based vaccine design, epitope mapping, antiviral development, and high-resolution imaging using cryo-EM and focused ion beam (FIB) milling.

Dr Eugene Krissinel leads the Macromolecular Crystallography Group within the Scientific Computing Department at STFC, UK. His group is responsible for the maintenance, development, and distribution of the CCP4 Software Suite, a cornerstone toolkit in protein crystallography. From 2000 to 2009, Dr Krissinel worked at the Protein Data Bank in Europe (PDBe) – formerly known as the Macromolecular Structure Database (MSD) – at the European Bioinformatics Institute, Hinxton, UK. During this time, he became widely recognised within the structural biology community for his contributions to protein-protein interaction (PPI) and protein structure analysis. His software tools for PPI and oligomeric state prediction (PISA) and protein structure alignment (SSM and Gesamt) are now considered de facto standards in the field. Before his career in structural bioinformatics and crystallography, Dr Krissinel worked on the theory of time-resolved diffusion and spin control in radical reactions, quantum kinetics (1997-2000 Humboldt Fellow, University of Konstanz, Germany, 1989-1995 Russian Academy of Sciences), and molecular dynamics of metallic alloy microclusters (1995-1997 Argonne National Laboratory, USA).

Flora Meilleur is a structural biologist specialized in protein chemistry and neutron crystallography. She is an instrument scientist on the single crystal macromolecular diffractometers, IMAGINE and MaNDI (HFIR CG-4D and SNS BL-11B), at Oak Ridge National Laboratory (ORNL). Meilleur received her PhD in biophysics from the European Molecular Biology Laboratory (EMBL) and Université Grenoble Alpes (Grenoble, France) in 2004. After graduating, she served as instrument scientist on the LADI diffractometer at the Institut Laue Langevin (ILL). She joined ORNL in 2005 and has held a joint faculty appointment with the Biochemistry department of North Carolina State University (NC State) since 2007. She is a Full Professor at NC State since 2023. In 2009, Meilleur lead a university consortium that secured NSF funding to build, commission and operate the IMAGINE instrument at HFIR. Until 2025, she supported and collaborated with research groups to elucidate enzymatic mechanisms using neutron diffraction on IMAGINE. This instrument has now been decommissioned to be replaced with a Dynamic Nuclear Polarization (DNP-)capable diffractometer (IMAGINE-X, under construction). Meilleur’s own research focuses on polymer degrading enzymes, including lytic polysaccharide monooxygenases and nylon hydrolases. Techniques used in her research group include X-ray/neutron crystallography, DFT calculations, small angle X-ray/neutron scattering and isotopic labeling techniques to study the structure, function and dynamics of these systems. Meilleur currently serves as a Main Editor for the IUCr Journal of Applied Crystallography.

Tzviya Zeev-Ben-Mordehai is an associate professor at Bijvoet Centre for Biomolecular Research of the Utrecht University in the Netherlands. She is an expert in cellular structural biology of mammalian gametes. Zeev-Ben-Mordehai was awarded her PhD in Structural Biology in 2008 from the Weizmann Institute of Science in Israel. For her postdoctoral training she moved to Oxford University to specialise in cryo-electron tomography (cryo-ET) and multi-modality, integrative structural biology. In 2015 she established her group also in Oxford University, her group combines biochemistry, biophysics, advanced cryo-EM methods and cross-linking mass spectrometry to unravel the molecular basis of fertilization. In 2017 she relocated her group to Utrecht University. Her group has pioneered the use of cryo-ET and cryo-EM to study mature mammalian sperm at the molecular level (EMBO J 2021, Nat Comm 2021, PNAS 2021). By developing a ‘cellular’ cryo-EM single-particle-analysis approach that allows resolving atomic resolution structures of multi-protein complexes without isolating them from the cell, we identified >180 proteins decorating sperm DMTs (Cell 2023, Nature 2025). Zeev-Ben-Mordehai is a recipient of a Wellcome Trust and The Royal Society Sir Henry Dale Fellowship (2015), NWO START-UP (2018), ERC-consolidator grant (2023) and NWO-Vici grant (2025).

Dr. Gaia Pigino is the Associate Head of the Centre for Structural Biology of the Human Technopole in Milan, Italy. At the forefront of structural and molecular cell biology, her team employs cutting-edge methodologies from both disciplines to investigate the molecular machinery essential for the assembly and functioning of motile and primary cilia. Gaia received her PhD in Evolutionary Biology from the University of Siena, Italy in 2007 for her studies of bio-indicators of contaminated soils. Electron microscopy (EM) quickly became central in her research. Following a brief postdoc at the EM Lab, University of Siena (2007-2009), where her fascination with cilia biology began, Gaia moved to Switzerland where she worked at ETH Zurich and Paul Scherer Institute (PSI) to investigate the structure of ciliary components using cryo-EM (2009-2012). In 2012, Gaia became a research group leader at the Max Planck Institute of Molecular Cell Biology and Genetics (MPI-CBG) in Dresden, Germany, before making her transition to the Human Technopole in Milan in 2021. The Pigino Lab adopts a multifaceted approach by integrating data from advanced in situ cryo-electron tomography (cryo-ET) with approaches such as AlphaFold protein structure prediction, structural proteomics, correlated light and electron microscopy (CLEM), expansion microscopy, spatial ‘omics, genome engineering, live imaging, and mechanical cell micromanipulations. Through this integrated approach, the lab has unveiled the molecular structure of Intraflagellar Transport (IFT) and explained several aspects of dynamics, and underlying mechanisms of this universally conserved bidirectional transport system, required for the assembly of cilia and eukaryotic flagella across all ciliated cells.

Venki Ramakrishnan has a long-standing interest in ribosome structure and function. His work led to the first high-resolution structure of the small ribosomal subunit, and was followed by structures of functional complexes of the entire ribosome in different states along the translational pathway. In the last decade, his lab has been applying cryoelectron microscopy to study eukaryotic and mitochondrial translation, particularly initiation of translation and its regulation. Since 1999, he has been on the scientific staff of the MRC Laboratory of Molecular Biology in Cambridge, England. He is the author of two popular books: Gene Machine and Why We Die.

Born in Detroit Michigan, Chris attended the University of Notre Dame where he obtained degrees in electrical engineering and philosophy. He then went to graduate school at Harvard and MIT, where he studied physics and medicine in the HST program under advisors Jene Golovchenko (Physics, Engineering) and Daniel Branton (Biology). There he developed a way to create nanopores in graphene with atomic precision, and technologies he developed during this time for high-speed DNA sequencing are now licensed to Oxford Nanopore. Chris moved to the MRC Laboratory of Molecular Biology (LMB) in 2011 when he joined Lori Passmore’s group to work on electron cryomicroscopy in biology. Chris became an Independent Investigator Scientist at the LMB in 2016 and a Group Leader in the LMB’s Structural Studies Division in 2018. Since becoming an independent investigator, he has remained focused on improving electron cryomicroscopy of biological specimens. Chris’s group works on developing new instruments and methods for imaging biological molecules, with the aim of improving cryo specimen preparation and imaging to the point where the electron microscope can be used to image the atomic resolution structure of all purified macromolecular complexes and the also determine the sub-nanometer precision structure of molecules in situ. Chris’s group draws on recent developments in microfabrication, solid-state physics, surface chemistry, electrical engineering and materials science to achieve these improvements.

Dr. Johannes Schwab completed his studies in mathematics at the University of Innsbruck (UIBK) and conducted his PhD research in inverse problems and machine learning under Prof. Markus Haltmeier in the Department of Mathematics at UIBK . His doctoral and postdoctoral research at the Medical Research Council (UKRI) / MRC Laboratory of Molecular Biology, spanned interdisciplinary topics such as tomographic reconstruction, denoising in imaging using deep learning, and cryo EM reconstruction methods, bridging applied mathematics with biophysical imaging . Now a Lecturer in Data Science & Intelligent Analytics at the University of Applied Sciences in Kufstein, Tirol (Austria) Johannes contributes to pioneering work in structural biology imaging analysis, focusing on methods like DynaMight, a deep-learning approach to estimate molecular motions from cryo EM data (2024), as well as self supervised strategies for image reconstruction in inverse problems such as computed tomography (2025).

Ioannis Skalidis is a structural biochemist with expertise in cryo-electron, integrative structural biology, and the analysis of large macromolecular assemblies. He earned his PhD in Biochemistry from Martin-Luther University Halle-Wittenberg, where he led research on the structural organization of endogenous protein complexes and metabolons using AI-enhanced cryo-EM, combined with integrative modelling approaches. He currently holds a postdoctoral position at Utrecht University’s Bijvoet Centre, focusing on the structural biology of ER protein biogenesis and translocation, using cryo-ET and modelling at scales. Ioannis combines laboratory skills, including cryo-EM sample preparation, and proteomics data analysis, with a strong background in computational structural biology, integrative modeling, AI-based structure prediction, and structural data interpretation. His research goals lie at the interface of molecular structure and systems biology, aiming to decipher the functional architecture of protein communities in a close-to-native context.

Weston is an Associate Professor in the Department of Biochemistry at the University of Oxford and Tutorial Fellow at Worcester College. He is also a UKRI Future Leaders Fellow and Group Leader in the Kavli Institute for NanoScience Discovery where his group studies the molecular mechanisms by which viruses, mainly HIV-1 and Ebola, glycosylate their surface proteins and the biophysics involved in host cell attachment, entry and antibody-mediated neutralisation. The group aims to pin-point how glycans modulate multivalent interactions involved in infectivity and immune responses. The group uses a rage of mass spectrometry methods, from glycomics and glycoproteomics to hydrogen-deuterium exchange and native mass MS. The group also develops mass photometry - a single molecule mass imaging technique established in the University of Oxford and the basis of Refeyn where Weston was Chief Scientific Officer from its founding. Weston has been in Oxford since 2012, in both the Chemistry and Biochemistry Departments as a Post-Doctoral Researcher and Senior Research Associate. Prior to moving to Oxford, he worked at the newly formed National Institute for Research and Training (NIBRT), a non-profit institute established to support research and education in biopharma globally. Weston his undergraduate degree from the University of Wisconsin, Madison and Ph.D. from the University of New Hampshire.

Paolo Swuec is a biochemist interested in the architectural characterisation of cellular and molecular targets by electron microscopy. After receiving a Ph.D. in Structural Biology at The Francis Crick Institute (UK), he joined University of Milan to set up and manage the first Cryo-Electron Microscopy Laboratory of the country. In 2020, he has been appointed Head of the Cryo-Electron Microscopy Facility at Human Technopole, a Facility he designed and built from scratch. In 2023, he has been appointed Head of the National Facility for Structural Biology, a state-of-the-art platform that provides access to integrative structural biology workflows for the entire national community. During his career, Paolo has made important contributions to the understanding of protein machineries involved in several key biological processes as DNA repair and replication, viral integration, and gene editing. He has also been involved in many tutoring, teaching and outreach activities to promote molecular biology and electron microscopy to general public and specialised audiences.

Dr. Andrea Thorn completed her studies in Molecular Life Sciences at the University of Erlangen Nürnberg and earned her PhD from the University of Göttingen, focusing on practical methods for macromolecular X ray structure determination in George Sheldrick’s group. She then contributed to crystallographic methods development at the University of Cambridge in the group of Randy Read. As a Marie Skłodowska Curie fellow at the MRC Laboratory of Molecular Biology she expanded her work into Cryo-EM and AI-based tools like HARUSPEX, pioneering automated interpretation of cryo-EM density maps through neural networks. This was soon followed by her software for diffraction data diagnostics, AUSPEX, which combines machine learning and visual diagnostics. She became a group leader in 2019. In 2020 she started and led the Coronavirus Structural Task Force, delivering critical structural evaluations of SARS-CoV-2 proteins and earning awards like the Max von Laue Prize 2022 and the Teaching Award of the City of Hamburg. Her group in the "Cluster of Excellence CUI: Advanced Imaging of Matter" in Hamburg worked both experimentally, as well as developing computational methods. Besides methods development and structural biology, she is interested in the biochemistry of fungi and lectures on human-made accidents. In early July 2025 she became a head of a new department "AI and biomolecular structures" at Helmholtz Center Berlin.

Christian Tüting studied biochemistry at Martin-Luther-University Halle-Wittenberg. For his PhD he joined the lab of Prof. Wahle in 2015, focusing on the polyadenylation of mammalian mRNA, a crucial two-step process involving a dozen distinct proteins and RNA-signal elements. To obtain low-resolution structural information on the underlying complexes, he applied cross-linking mass spectrometry. In 2019, he then joined the newly founded laboratory of Prof. Kastritis at the same university and was a key part of establishing the first state-of-the-art cryo-EM laboratory in eastern Germany. There he gained insights into the native pyruvate dehydrogenase complex and built an integrative workflow combining cryo-EM density with molecular docking, energetic refinement, molecular-dynamics simulations and biochemical knowledge. Since the release of AlphaFold, incorporating AI-driven models has become an essential element of his work, further extending the capabilities of integrative structural biochemistry.

Dr. Brinda Vallat received her Ph.D. in Molecular Biophysics from the Indian Institute of Science in Bangalore, India. She moved to the US and continued her postdoctoral research in the field of computational biology and bioinformatics, where she worked on developing methods for modeling and analysis of biomolecular structures. In 2015, she joined Rutgers, the State University of New Jersey, as a research associate. She is currently an Associate Research Professor at the Institute for Quantitative Biomedicine at Rutgers and a member of the RCSB Protein Data Bank (PDB). Her research aims at making structural biology data Findable, Accessible, Interoperable, and Reusable (FAIR) and building tools for data standardization, curation, validation, and dissemination. She is currently working on developing the PDB-IHM system for archiving structures of biological macromolecules determined using integrative structure determination methods. Recently, PDB-IHM was unified with the PDB to make integrative structures available alongside experimental structures in the PDB.

Dr. Ellen D. Zhong is an Assistant Professor of Computer Science at Princeton University, where she leads the E.Z. Lab for Molecular Machine Learning. She joined Princeton in July 2022, following her PhD in Computer Science at MIT (2022), during which she developed cryoDRGN—a deep learning system for reconstructing dynamic protein structures from cryo EM data . Her prior experience includes work at D. E. Shaw Research on molecular dynamics algorithms for drug discovery and an internship with the AlphaFold team at DeepMind . Dr. Zhong’s research lies at the intersection of AI and structural biology, focusing on image analysis and 3D reconstruction to map protein structure, dynamics, and interactions. Her group recently introduced CryoDRGN ET (Nature Methods, June 2024) and CryoDRGN-AI (Nature Methods, June 2025), neural reconstruction methods for visualizing heterogeneous molecular states inside cells, and continues to innovate in algorithmic methods with applications bridging AI and experimental biology . She holds affiliations with Princeton’s Center for Statistics and Machine Learning, Princeton Laboratory for Artificial Intelligence, and the Omenn Darling Bioengineering Institute.

Monica Zoppè completed her studies in biology at the University of Milan, in 1987. She then spent the next 20 y doing wet research in laboratories in Italy and abroad, including the University of Birmingham, UK, the Salk Institute in San Diego, CA, the International Center for Genetic Engineering and Biotechnology (ICGEB), in Trieste, and the Institute of Clinical Physiology of CNR in Pisa, Italy. She is now at the Institute of BioPhysics of the National research Council of Italy in Milan. In the early 2000s , following an accident, she left the wet research and started to dedicate to representation of structural and cellular data, using the tools of Computer Graphics, for which she developed, with the Scientific Visualization Unit, the program BioBlender, and AddOn for Blender, one of the most versatile and popular programs in CG, completely free and Open. Using the program, the group prepared several short video animation, all available on the SciVis.it webpage. During this time, Monica also contributed to theoretical aspects of visualization and representation, and is now considered a pioneer and an expert in the field.