Bob obtained his BSc (1987) from King’s College, London University, his MSc (1990) from University of British Columbia, his DPhil (1996) from Oxford University and his postdoc was completed at the Salk Institute for Biological Studies (1996-2001). During his postdoctoral studies, Bob was prominent in solving the structure of arp2/3, a seven-protein, actin-nucleating complex. In 2001, Bob was appointed as a Senior Lecturer at Uppsala University. There, Bob’s research group continued to elucidate structures of key actin regulating proteins such as gelsolin and thymosin-?4. He joined IMCB in 2005 as an Associate Professor and Principal Investigator.

A macrophage moving towards a site of infection or a developing (or regenerating) neuron extending towards its target tissue are just two examples where an enhanced knowledge of the molecules involved in cellular locomotion will contribute towards the greater understanding of cell behaviour.

The main aim of Dr. Robinson’s laboratory is to seek a detailed knowledge of the mechanisms behind cell motility, through elucidating the structures of key components of the actin motility machine. Movement is a defining characteristic of life. Macroscopic motion is driven by the dynamic interactions of myosin with actin filaments in muscle. Directed polymerization of actin behind the advancing membrane of a eukaryotic cell generates microscopic movement. Despite the fundamental importance of actin in these processes, the structure of the actin filament remains unknown. A structure determination is often critical to understanding a protein’s function, and currently, only hypotheses as to the actin filament structure are available. In isolation, actin filaments are not amenable to crystallization due to their non-homogeneous length distribution. Fortunately, a myriad of actin-binding proteins exist that can modify actin filaments. Some proteins cap filaments, some stabilize filaments, whilst others sequester small numbers of actin protomers. The short-term goal of Dr. Robinson’s research group is to determine the structure of actin in complex with a range of these proteins, proteins that are biologically and medically interesting in their own right. From the resulting database of actin interactions the appropriate actin-binding modules will then be combined to create novel, engineered proteins that stabilize actin mini-filaments, ultimately allowing the actin filament structure to be determined. This innovative approach to structural biology will create the tools to allow the structure determination of even more complicated geometries, such as the arp2/3 branched actin filament. Together these structures will reveal mechanisms behind actin filament assembly and molecular motion.

The Robinson laboratory specializes in protein crystallography. This method that allows elucidation, at atomic resolution, of the high molecular weight complexes involved in cell motility. From the conformations of the determined protein complexes they attempt to understand how each protein performs its biological function. The Robinson laboratory focuses on proteins that undergo large conformational changes, proteins that are required to be structurally dynamic in achieving cellular motion, and work almost exclusively with protein complexes rather than single proteins. This adds an extra level of difficulty to the discipline, as protein complexes and proteins with multiple conformations have to be stabilized in a particular form with an exact stoichiometry in order to crystallize. However, more importantly, the approach maximizes the biological significance of the results. The laboratory also uses TIRF microscopy and SAXS techniques to supplement the crystallography data in order to provide a dynamic view of protein complexes.