'The century of vision: Protein structures in basic science and pharma research'
Robert Huber was awarded the Nobel Prize for Chemistry in 1988. He was Director at the Max Planck Institute for Biochemistry in Martinsried until his retirement in 2005 and is currently a professor at the Technische Universität München (TUM). Dr. Huber has made major contributions to the understanding of the structure and function of biological macromolecules. In addition, he has contributed to the development of protein crystallography, particularly Patterson methods, graphic methods, and refinement, and most recently to methods and instruments for crystal improvement. He is co-founder of two companies, Proteros and Suppremol. In addition to the Nobel Prize, he has been honoured by numerous honorary doctorates, professorships, memberships in learned societies including NAS, and awards including the Otto-Warburg Medal, the Emil von Behring Medal, the Sir Hans Krebs Medal, the Linus Pauling Medal, and the Max Tishler Prize.
'MicroED: conception, practice and future opportunities'
Dr Gonen is a Member of the Royal Society of New Zealand, a Professor of Biological Chemistry and Physiology at the David Geffen School of Medicine of the University of California, Los Angeles and an Investigator of the Howard Hughes Medical Institute. He is an expert in electron crystallography and cryo EM, determining the 1.9Å resolution structure of the water channel aquaporin-0 by electron crystallography, the highest resolution for any protein determined by cryo EM techniques at the time. Since 2011, Dr Gonen has worked as a Group Leader at the HHMI Janelia Research Campus where he has continued to work in electron crystallography, pioneering MicroED, a structural biology method with the potential to solve unknown structures at resolutions close to 1Å.
Protein preparation for structure biology in industrial settings is in transition as new techniques are introduced. Our panel will discuss differences in protein requirements for X-ray crystallography versus Cryo-EM, stabilization techniques for membrane proteins maintaining the functional state, data bases as tool to efficient construct design, and offer attendees to ask detailed questions regarding upscale and purification approaches, most useful analytical equipment and new developments in supporting software.
Sujata Sharma (Janssen Research & Development) - Moderator
Byron DeLaBarre (Nimbus)
Kathleen Aertgeerts (Vertex Pharmaceuticals)
Additional panelists to be announced
There are a wide range of new technologies and techniques now available to explore the connections between protein structure and function. The recent availability of bright X-ray microbeams and advanced automation at synchrotrons, the use of high-speed pixel array detectors for diffraction and Cryo-EM measurements, and the advent of X-ray Free Electron Lasers (XFELs), has enabled the examination of biological systems that were previously inaccessible. Such procedures such as room temperature serial crystallography on nano-crystals, in-situ crystallization and diffraction screening, controlled dehydration and on-site integration of X-ray results with Cryo-EM are now becoming readily available to the industrial community. The panel will discuss how these advances will benefit the structural biologist in a drug discovery setting and will answer attendees' questions on where they see these multiple developments taking the industrial user in the future.