I became interested in structural biology as an undergraduate at the University of Oxford. This led me to start a PhD in 1999 with Venki Ramakrishnan at the MRC Laboratory of Molecular Biology in Cambridge.
I worked as part of the team that determined the X-ray crystal structure of the small (30S) ribosomal subunit. In addition I solved structures of the ribosome bound to antibiotics and the protein initiation factor IF1. After my PhD I spent an extra year in Cambridge as a junior research fellow at Clare College, before moving in 2003 to Ron Vale’s lab at the University of California where I started working on dynein. Together with Sam Reck Peterson I used S.cerevisiae to express a recombinant dynein motor for biophysical studies. I collaborated with the group of Ian Gibbons to solve the structure of dynein’s microtubule binding domain (2008) and together with Carol Cho produced the first crystal structure of the dynein motor domain (2010).
In 2008 I accepted a group leader position back at the MRC-LMB which I started in August 2010. My group initially focused on crystallography of the dynein motor domain, solving high resolution structures which revealed how ATP hydrolysis drives movement. We subsequently moved to asking how dynein works together with its cofactor dynactin to transport cargos, taking advantage of advances in cryoEM technology.