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Helen Saibil is a structural biologist at Birkbeck, University of London, where she built up a cryo electron microscopy lab. She was educated at McGill University, Montreal, and at Kings College London. Her research career started at Kings, then the Centre d'Etudes Nucléaires, Grenoble, and Oxford University, before settling at Birkbeck. Her research is on macromolecular machines, both in vitro and in their cellular context. A major focus is the action of molecular chaperones in assisting protein folding, unfolding and disaggregation. In addition, she studies the actions of intracellular pathogens and pore forming toxins on host membranes.

Werner Kühlbrandt 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 investigating the structure of membrane proteins, first at the ETH Zürich, and then at Imperial College London. As a research group leader at EMBL Heidelberg he determined the high-resolution structure of the plant light-harvesting complex LHC-II by cryoEM. Since 1997 he has been a director at the Max Planck Institute of Biophysics in Frankfurt, Germany, where his department of Structural Biology studies large membrane protein complexes primarily by single-particle cryoEM and electron cryo-tomography.
 

Thomas Braun studied biophysics at the Biozentrum of the University Basel, Switzerland, and completed his PhD 2002 on high-resolution electron microscopy of membrane protein channels and transporters. In his postdoc and senior researcher at the Physics Institute of Basel and the Trinity College Dublin (Ireland), he developed nanomechanical sensors for real-time analysis of biological processes. 2009 he returned to Basel to the Center of Cellular Imaging and Nanoanalytics (C-CINA) and now leads a research team at the Biozentrum of the University Basel. His group focuses on developing novel microfluidic sample-preparation methods for protein isolation, high-resolution electron microscopy, and “single-cell visual proteomics.”
 

I completed my PhD in Structural Biology, at the laboratory of Professor Helen Saibil in Birkbeck College, London. During my PhD I focused on membrane protein structure determination using 2D crystallography and cryo-EM. However the lack of crystalline order necessitated the application of single particle averaging methods and this work was performed in collaboration with Elena Orlova. After my PhD I continued to work in Professor Saibil’s laboratory but switched entirely to single particle analysis and applied cryo-EM to molecular chaperones to elucidated some of the first substrate bound and ATP triggered structures of GroEL. In 2015 I moved to Diamond Light Source to set up and co-manage the new national cryo-electron microscopy facility, eBIC. Currently the facility comprises seven state-of-the art cryo-electron microscopes, four of which are running full internationally recognised external user programs. Data collected at eBIC, using a free-at-the point of access model, has been crucial in number of high impact publications from UK and European based scientists. During my time at Diamond I have maintained my research interests predominantly working on the chlamydia infection of mammalian cells using cryo-FIB milling and electron tomography. I currently have a joint PDRA with the membrane protein lab at Diamond looking at optimising membrane protein structure determination by cryo-EM. As well as this I am involved in a number of collaborations with Rosalind Franklin institute and industrial partners looking at the next generation cryo-EM and freezing devices.

Born in Detroit Michigan, Chris attended the University of Notre Dame where he studied electrical engineering and philosophy. He then went on to graduate school at Harvard and MIT, where he studied physics and medicine under the supervision of Jene Golovchenko (Physics, Engineering) and Daniel Branton (Biology). During this time, he developed a new technique to create nanopores in graphene with atomic precision that combined ion bombardment with high energy electron irradiation.

He then moved to the MRC Laboratory of Molecular Biology in Cambridge, UK, to work on developing new methods for electron cryomicroscopy (cryo-EM). Chris has since started his own group at LMB, and continues to study the physical phenomena that limit resolution in cryo-EM and thus enable the development of new devices, instruments and methods to improve the imaging power of the electron microscope in biology.

Sjors studied chemistry at Utrecht University, The Netherlands, where he also obtained his PhD in protein crystallography. He was a post-doc in the group of Jose-Maria Carazo in Madrid, before he started his group at the LMB in 2010. Since 2018, Sjors is also joint Head of the Structural Studies division. His main interests lie in the development of new methods for high-resolution cryo-EM structure determination, and their application to amyloid filaments. Sjors is the main author of the RELION program for cryo-EM structure determination, and he solved numerous structures of amyloid filaments, among others of the proteins tau, alpha-synuclein and amyloid-beta.

Rebecca is the Head of Faculty Biological Sciences Research Facilities and Deputy Director Asbury Biostructure Laboratory, University of Leeds. In this role she oversees delivery of range of research facilities, including cryo-electron microscopy capabilities with two state-of-the-art Titan Krios microscopes. Her current research interests span cryo-electron microscopy and include developing and optimising workflows for high resolution structure determination of macromolecular complexes by single particle analysis and using cryo-electron microscopy to image protein:membrane interactions. 
 

After undergraduate studies in Italy and Australia, Giulia completed her PhD in Oxford (2004-2009), working on cryo-tomography studies of viral glycoproteins. After a postdoc at the University of California, Berkeley, she joined the Institute of Structural and Molecular Biology (ISMB) at Birkbeck College in London. In 2014 Giulia was awarded a Dorothy Hodgkin Royal Society fellowship, which kick-started her lab. Currently her group is pushing the boundaries of cryo-tomography to understand mechanisms of complex membrane trafficking processes. Integration with biochemical techniques and collaboration with labs who use complementary approaches is helping to understand how the COPII coat remodels membrane and how this process is regulated.