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.