Committees

Program

Speakers and Tutors

Bursaries

Registration

Venue

foto 1 Follow news and updates also on the AIC Facebook page!

For any queries please contact the Organizing Committee at aicschool@cristallografia.org

Organized by


AICS 2017 Confirmed Speakers and Tutors


Wayne A. Hendrickson (Columbia University, US) is a University Professor at Columbia University. He has a B.A. in physics and biology from the University of Wisconsin at River Falls and a Ph.D. in biophysics from Johns Hopkins University, which was based on work with Warner Love. His postdoctoral research was with Jerome Karle at the Naval Research Laboratory (NRL). He remained at NRL as a Research Biophysicist until 1984 when he joined the Department of Biochemistry and Molecular Biophysics at Columbia. Hendrickson was also an HHMI Investigator from 1986 to 2012; in 2008, he was named the Violin Family Professor of Physiology and Cellular Biophysics at Columbia; and in 2010 he became the Scientific Director of the New York Structural Biology Center. Hendrickson and his colleagues use x-ray crystallography, cryogenic electron microscopy (cryo-EM), and biochemical analyses to study biological macromolecules in atomic detail. Their advances in diffraction methods (notably, stereochemically restrained refinement, phase evaluation from anomalous diffraction, selenomethionyl proteins, and synchrotron instrumentation) have been instrumental in the emergence of structural biology as a major force in modern biology and molecular medicine. Their biological applications include investigations on membrane receptors and cellular signaling, on viral proteins and HIV infection, on molecular chaperones and protein folding, and in structural genomics of membrane proteins. Hendrickson has published numerous scientific articles. He serves on advisory bodies for various scientific organizations. He is a founding editor of Current Opinion in Structural Biology and of Structure, and he was a founder of SGX Pharmaceuticals. His honors include the Aminoff Prize of the Royal Swedish Academy of Sciences, the Canada Gairdner International Award, and the Harvey Prize of the Technion – Israel Institute of Technology. He is a fellow of the American Academy of Arts and Sciences and a member of the National Academy of Sciences.


Werner Kuhlbrandt (Max Planck Frankfurt, Germany) studied chemistry and crystallography at the Free University Berlin, and biochemistry and biophysics at King’s College London. He did his PhD with Nigel Unwin at the MRC Laboratory of Molecular Biology in Cambridge, UK, investigating the structure of two-dimensional ribosome crystals by electron microscopy. As a postdoc, he turned to structural studies of membrane proteins, first at the ETH Zürich, and then at Imperial College London, to determine the high-resolution structure of the plant light-harvesting complex, LHC-II. After a short stay at UC Berkeley, CA, he became a group leader at EMBL Heidelberg in 1988, where he solved the cryoEM structure of LHC-II at 3.4 Å resolution. Since 1997 he is a director at the Max Planck Institute of Biophysics in Frankfurt, Germany. His department of Structural Biology investigates the structure and function of membrane transport proteins by X-ray or electron crystallography, and the structure of large membrane protein complexes, such as the mitochondrial ATP synthase, by single-particle cryoEM and electron tomography.


Fabrizio Martino (CIB Madrid, Spain)


Arjen J. Jakobi (EMBL Heidelberg, Germany) studied Molecular Sciences at Leiden University (NL) and the University of Erlangen (DE), where he majored in computational chemistry and structural biophysics. After developing quantum-based methods for rational drug design at F. Hoffmann – La Roche in Basel (CH), he trained in X-ray crystallography during his PhD with Piet Gros and Eric Huizinga at Utrecht University where he determined the structural basis for force-sensitive activity regulation of the giant shear sensor protein von Willebrand Factor. In 2012 he moved to EMBL Heidelberg as an EIPOD postdoctoral fellow. At EMBL he focuses on elucidating the structure of large macromolecular assemblies in selective autophagy using cryo-EM and on method development in cryo-EM and X-ray crystallography. He has a particular interest in image processing algorithms for the reconstruction of helical specimen and the improvement of methods for atomic model refinement against high-resolution cryo-EM density maps. He will soon be setting up a cryo-EM research group at the Kavli Institute for Nanoscience and Department of Bionanoscience at Delft University of Technology (NL).


Tillmann Pape (Imperial College London, UK) first became fascinated with cryo-electron microscopy and single particle analysis during his PhD more than 20 years ago. After 8 years of PhD work on different molecular machines, he decided take the opportunity to become more involved with the technology itself, the training of its varied users and the management of a cryo-EM facility. To this day, he enjoys tremendously the interaction with people from different scientific backgrounds and introducing, supervising and consulting them in this beautiful structural technique in the effort to explain biological function.


Christoph A. Diebolder (NeCEN, NL)


Marta Carroni (SciLife Lab, Sweden) is Head of the Cryo-EM National Facility Stockholm node at SciLife Laboratory, Sweden. She joined as a staff member of the Department of Biochemistry and Biophysics at Stockholm University, after receiving a PhD in Structural Biology at Imperial College London and a postdoc in electron microscopy at Birkbeck College London, UK. During her PhD she worked on the structural characterization of transcription and replication factors, by using different biophysical and biochemical assays as well as electron microscopy. For her postdoc she joined Helen Saibil’s group where she worked on cryo-EM structures of AAA+ molecular chaperones. This is still her main research interest besides the running of the National Facility. She has been involved as a tutor in various editions of the EMBO course on EM image processing and she organized a pilot course for single particle EM at Stockholm University. She enjoys the possibility that the Facility offers of working with large number of scientists and on a variety of projects.


Mauro Gemmi (IIT Pisa, Italy) is Director of the Center for Nanotechnology Innovation in the Italian Institute of Technology, an interdisciplinary R&D center dedicated to the investigation and exploitation of phenomena at nanoscale level. As physicist with expertise in transmission electron microscopy, he is a pioneer in the use of precession electron diffraction for solving crystal structures and one of maximum experts in electron crystallography. Mauro Gemmi past experience includes research activities in new electron crystallography methods in Sweden (University of Stockholm), solid properties of minerals under non ambient conditions (HT, HP) developing new methods for solving structures with electron diffraction data in Italy (TEM Lab of Earth Science Dep., University of Milan), as well as Invited Scientist in France (CNRS-Institute Néel in Grenoble) for developing methods for solving structure using the new precession electron diffraction technique. He is responsible for the both the material science and biology research carried out in the TEM lab of CNI. He is chair of the special interest group no electron crystallography (SIG4) of European Crystallographic Association.


B. Tom Burnley (CCP-EM,STFC, UK) is a computational scientist working for the Science and Technology Facilities Council (STFC) since 2013. He is based at the Harwell Research Campus, Oxfordshire, UK and works on the Collaborative Computational Project for Electron cryo-Microscopy (CCP-EM) project. This role involves: a) development and dissemination of CryoEM software; b) providing training for users; and c) computational support for our partner collaborators. He has developed the CCP-EM software framework to link, test and distribute ancillary programs together (programs include Refmac, Molrep, MRC Image Processing Software, DockEM, FlexEM, TemPy and Relion). Previous to this he was a PostDoc with Piet Gros, Utrecht University, focusing on refinement algorithms for x-ray crystallography, developing ‘phenix.ensemble_refinement’.


Alessandro Vannini (ICR, UK) studied Biology at the University of Rome "Roma Tre" and undertook his Ph.D. research at IRBM "P. Angeletti" (Merck Research Lab), Rome, focussing on the structural characterisation of quorum-sensing proteins in pathogenic bacteria and of human histone-deacetylases (HDACs). For his post-doctoral research, supported by Marie-Curie and EMBO long-term fellowships, he joined Professor Patrick Cramer's laboratory in Munich, focussing on the architecture and regulation of yeast RNA polymerase III, the largest among the three eukaryotic RNA polymerases, by combining X-ray crystallography and cryo-electron microscopy. In 2012, Dr Alessandro Vannini joined the Institute of Cancer Research in London, UK, as Team Leader in the Division of Structural Biology. Using an Integrative Structural Biology approach, he and his team are focusing on the structural and functional characterisation of large macromolecular complexes that assemble at RNA polymerase III binding sites across the eukaryotic genome, in order to understand their role in tumorigenesis as well as in the 3D spatial organization of the genome. In 2016, Dr. Vannini was elected EMBO Young Investigator and Wellcome Trust Investigator.


Paolo Swuec (University of Milano, Italy) is facility manager of the newly established Cryo-Electron Microscopy Lab, a joint research centre between the Paediatric Clinical Research Centre Romeo and Enrica Invernizzi and University of Milan. He joined Prof. Martino Bolgnesi’s group in March 2017 as PostDoc after receiving a Ph.D. in Structural Biology at The Francis Crick Institute, UK. During his Ph.D. he focused on the architectural characterization of macromolecular machines involved in DNA repair by a combination of protein biochemistry, biophysics and electron microscopy. He also made contributions to the understanding of protein machineries involved in DNA replication and viral DNA integration. He has been involved in tutoring, teaching and outreach activities to promote molecular biology and electron microscopy.


Guy Schoehn (IBS Grenoble, FR) is Head of the Integrated Structural Biology Grenoble Institute EM platform (UMS 3518 CNRS-CEA-UJF-EMBL) and Group leader at the Structural Biology Institute (IBS) in Grenoble). The group Electron Microscopy and Methods composed of four teams and 20 people is also running the ME Platform. The group is interested in the structure of macromolecular assemblies in general and viruses in particular. One of the aims of the team is also the development and spreading of the use of electron microscopy in structural biology at the local and the national level. Guy Schoehn is also President of the French Microscopy Society. He is member of the International Scientific Advisory Board 5Lyon 2016 and Copenhague 2020) and of the Local Organizing Committee for the European Microscopy Congress 2016 (Lyon).


Martin Walsh (Diamond eBIC, UK). His research is focused primarily on understanding the mechanisms used by respiratory bacterial pathogens to adhere to host cell surfaces, regulation of biofilms and carbohydrate/nutrient uptake (ABC transporters). He is deputy to the director of life sciences at Diamond Light Source (DLS) and has been a key player in the instigation and implementation of high-throughput methods for structural biology, in particular automation of sample handling, standardisation of workflows and development of ISPyB for sample management. He has been intimately involved in the establishment of the UK’s X-FEL hub at Diamond and the associated SFX/SPB instrument at the European X-FEL in Hamburg as well as playing a key role in the establishment of eBIC the UK’s national CryoEM centre. He has over 25 years’ experience in macromolecular X-ray crystallography (MX) and has deposited >90 structures with the Protein Data Bank.


Filippo Mancia (Columbia University, US) is an Associate Professor in the Department of Physiology & Cellular Biophysics at Columbia University. He graduated in Chemistry in Pavia (Italy), and obtained a PhD at the MRC Laboratory of Molecular Biology in Cambridge, UK. His post-doctoral work was carried out in the labs of Drs. Wayne Hendrickson and Richard Axel at Columbia University. He is a structural biologist with experience in x-ray crystallography, single particle cryo-EM, and in production and characterization of membrane proteins for structural studies. The main research focus of his lab is on membrane protein – lipid interactions, both in terms of enzymes, which process lipid substrates, and of transporters, which mediate cellular uptake of lipidic substrates. He has also been a key member of the New York Consortium of Membrane Protein Structure (NYCOMPS), where he has played a pivotal role in the design, development, implementation and optimization of the high-throughput cloning and protein production platform for prokaryotic membrane proteins successfully functioning at the NYCOMPS center. NYCOMPS has recently transitioned to a NIH-funded biomedical technology resource center named the Center on Membrane Protein Production and Analysis (COMPPÅ; Wayne Hendrickson, PI), and he serves on the executive committee for COMPPÅ.


Pablo Conesa (I2PC Madrid, Spain) has a degree in Biology and for more than 15 years he is being working and trained in the software development industry. More recently (last 6 years) he made a strategic move to work in the academia, first at European Bioinformatics Institute (EBI), in Cambridge, and currently at the INSTRUCT Image processing center (I2PC) in Madrid. He is currently the technical leader of Scipion, an image processing framework to obtain 3D models of macromolecular complexes using Electron Microscopy, integrating several EM software packages and presenting a unified interface for both biologists and developers. His background in biology, his master in Bioinformatics from the UCM (Madrid University) and his wide experience in software engineering makes him suitable for producing good software while understanding the biology domain.


Ludo Renault (NeCEN, NL) is NeCEN’s facility manager since February 2016. After following a University education in Integrative Biology, he obtained a Master’s degree in bio-informatics and structural biology, and then a PhD in Neurosciences using X-ray crystallography as the main structural biology technique from Marseille University, France. He then joined Prof. Henning Stahlberg’s laboratory at UC Davis CA, USA as a post-doctoral researcher in high-resolution cryo-TEM where he performed single particle studies of DNA-binding proteins and obtained and imaged different 2d crystals of membrane proteins. He then moved to Canada to join Prof. Howard Young at the University of Alberta to perform 2D and 3D crystallization of membrane proteins of interests as well as performing single particle studies of prion fibrils. In 2012 he joined CRUK (now part of The Crisk) as a cryo-EM specialist to contribute to develop the cryoEM single particle approach.

+ Presentations from technical specialists:
- Max Maletta (FEI)
- Andy Jarwood (JEOL)
- Sacha De Carlo (Dectris)
- Frederic Leroux (Leica Microsystems)





© 2017 AIC - Associazione Italiana Cristallografia