**About the Editor**

### **Chrisostomos Prodromou**

Chrisostomos Prodromou obtained a first-class honours degree in Applied Biology at Chelsea College, University of London, and a PhD in Yeast Molecular Genetics from Queen Mary College, University of London, in 1988. Following a brief spell at the University of Sheffield, he then moved to University College London in 1991, where he started working on the molecular chaperone Hsp90. Chris continued his work on Hsp90 at the Institute of Cancer Research, which he joined in 1999. In 2010, Chris accepted a senior research fellowship at the University of Sussex, and later became senior lecturer, where he continues his studies on Hsp90. Chris' research interests over the last 20 years have been directed towards the structure and mechanistic action of the Hsp90 chaperone complex. Chris' aims are to understand the molecular details by which Hsp90 and its cohort of co-chaperones bring about the maturation and activation of its client proteins. His structure of the N-terminal domain of Hsp90 in complex with ATP won him the award for the best postdoctoral paper within a decade to be published in the Department of Biochemistry and Molecular Biology at UCL. This work showed that Hsp90 was an active ATPase and changed the course of research within the field. At the Institute of Cancer Research, Chris was involved in developing the resorcinol class of Hsp90 inhibitors, as well as a number of inhibitors of Hsp90 based on the natural antibiotics radicicol and geldanamycin. He also solved the structure of the full-length Hsp90 protein, giving us our first insight into the closed, N-terminally dimerised, conformation of Hsp90. At the University of Sussex, Chris solved the first structure of an Hsp90 in complex with a C-terminally bound Hsp90 activator, LA1011, which shows excellent potential as a clinical candidate against Alzheimer's disease. Chris, together with a number of his colleagues, is a holder of the 2013 CRUK translational prize towards beating cancer.
