Andrew P. Carter

Carter studied Biochemistry at the University of Oxford, graduating in 1999.[5] He obtained a PhD in 2003 from the MRC Laboratory of Molecular Biology where he worked with Venki Ramakrishnan on the ribosome. He was a member of the team in Ramakrishnan's lab that solved the first X-ray crystal structure of the small (30S) ribosomal subunit.[6] Carter also determined structures of 30S bound to antibiotics[7] and bound to the initiation factor IF1.[8] Ramakrishnan shared the Nobel prize in Chemistry for the team's work on the 30S.[9]

Carter was a post-doc in Ron Vale's lab[10] at University of California, San Francisco from 2003 to 2010. During his post-doc, he studied the molecular motor protein, dynein using X-ray crystallography and single molecule fluorescence microscopy.[11][12]

He became a group leader at MRC Laboratory of Molecular Biology in Cambridge in 2010 where he uses X-ray crystallography, electron microscopy, and single molecule microscopy assays to understand how dynein transports cargo. His group solved X-ray crystal structures of the dynein motor domain showing how it generates force to pull cargos along microtubules[1] and reconstituted a recombinant dynein, showing how its processive movement is activated by cofactors/cargo adaptors.[13] His group used cryoEM to solve the structure of dynein's cofactor dynactin[2] and the full length dynein complex.[3] They showed how dynein and dynactin come together in the presence of cargos and how this activates transport.