Andrew R. Marks, Columbia University
Rivka Carmi, President of Ben-Gurion University (BGU)
Montserrat Samso, (VCU)
Oliver Clarke, Columbia University
Filip Van Petegem, University of British Columbia
Ran Zalk, Ben-Gurion University
Irina Serysheva, University of Texas
Henry Colecraft, Columbia University
Marco Mongillo, University of Padova
Joachim Frank, Columbia University (Nobel Laureate)
Alexis Dudden, University of Connecticut
Yasser Hashem, University of Bordeaux
Amedee des Georges, City University of New York
Gabriel Frank, Ben-Gurion University
Varda Shoshan-Barmatz, Ben-Gurion University
Raz Zarivach, Ben-Gurion University
Beatrice Vallone, University of Roma
Ohad Medalia, University of Zurich, Ben-Gurion University
Meytal Landau, Technion
Natalie Ilia, Ben-Gurion University (BGU)
Itay Rousso, Ben-Gurion University (BGU)
Alex Kushnir, Columbia University
Wayne Hendrickson, Columbia University
High-Resolution Protein Structures: Understanding Human Diseases
Ben-Gurion University of the Negev, Israel
Ben-Gurion University, March 19 – 20, 2018
This meeting at The National Institute for Biotechnology at Ben-Gurion University will focus on the applicable sides of structural biology, in particular on how it helps understanding human diseases at the molecular level. Research scientists will highlight the state-of-the-art in structural biology.
Recent advances in cryo-electron microscopy have revolutionized the field of structural biology. It is now possible to achieve high-resolution structures of purified proteins and build de-novo models of biological macromolecules without the need for crystallization. Larger organelles and cell sections can also be visualized and detailed proteins structures can now be solved in their native environment with these newly available technologies. That said, X-ray crystallography is far from extinct. Atomic-resolution maps of medium and small-sized macromolecules still require X-ray crystallography to resolve a detailed structure. Furthermore, it is now becoming clear that complex structures may require more than one method to fully answer structural questions. We will discuss methods including crystallography, cryo-EM, Atomic force microscopy and super-resolution fluorescent microscopy.