Christopher Aylett
Structural biologist who solved the first cryo-EM architecture of human mTORC1 at ETH Zurich and now leads a cryo-EM group at Imperial College London
Section for Structural and Synthetic Biology, Department of Infectious Disease, Imperial College London (papers 2020–2026) · Institute of Molecular Biology and Biophysics, ETH Zurich (papers 2015–2018) · MRC Laboratory of Molecular Biology, Cambridge (2012 paper with Jan Löwe)
Portrait: ResearchGate
Christopher Aylett is first author of AYL2015, the first detailed 3D architecture of human mTORC1, made by cryo-electron microscopy (cryo-EM). The structure showed that mTORC1 is a dimer, two copies of mTOR, Raptor and mLST8 joined into a lozenge-shaped complex with the two kinase active sites sitting in deep clefts. That arrangement explains how the complex limits which proteins can reach the active site, and how the drug pair rapamycin-FKBP12 narrows the entrance further. Aylett is also a co-author of STU2018, the matching architecture of the mTORC2 core.
Aylett's earlier work, at the MRC Laboratory of Molecular Biology in Cambridge with Jan Löwe, was on bacterial proteins that push plasmids apart before cell division; a 2012 paper there described a DNA-protein filament at the heart of the TubZRC system. The mTOR structures came from a period at the Institute of Molecular Biology and Biophysics of ETH Zurich, working with Nenad Ban and Timm Maier.
Since about 2020 Aylett has led a group in the Section for Structural and Synthetic Biology of the Department of Infectious Disease at Imperial College London. The lab uses cryo-EM on large molecular machines, including the unusual RNA polymerase of the giant bacteriophage PhiKZ, a virus being explored as a treatment for Pseudomonas infections (2026), and develops simpler ways to prepare cryo-EM samples, such as a 3D-printed tool for moving fragile carbon and graphene support films.
Milestones in the Atlas
A selection, not a full bibliography: only papers that meet the Atlas inclusion criteria.
| Year | Evidence | Study |
|---|---|---|
| 2015 | M | Architecture of human mTOR complex 1 AYL2015 First author: determined the cryo-EM architecture of human mTORC1, a dimer with recessed active sites. |
| 2018 | M | Architecture of the human mTORC2 core complex STU2018 Co-author: contributed to the architecture of the human mTORC2 core complex. |
Co-authors in the Atlas 8
People with a profile here who share at least one study with Christopher Aylett.
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- Daniel Boehringer 2 shared studies Electron microscopy specialist at ETH Zurich whose cryo-EM work underpins the Atlas structures of human mTORC1 and mTORC2
- Evelyn Sauer 2 shared studies Structural biologist at the Biozentrum Basel who worked on the structure of the mTOR kinase and contributed to the cryo-EM structures of human mTORC1 and mTORC2
- Michael N. Hall 2 shared studies Discovered TOR in yeast in 1991 and established it as a central controller of cell growth that responds to nutrients. His lab later showed that TOR works in two distinct complexes, TORC1 and TORC2, only one of which is blocked by rapamycin
- Nenad Ban 2 shared studies Structural biologist known for atomic structures of the ribosome and for work on how cells make, fold and sort proteins.
- Stefan Imseng 2 shared studies Structural biologist from Timm Maier's group at the Biozentrum Basel who helped solve the first detailed structures of human mTORC1 and mTORC2 and then worked on a drug to block mTORC1 specifically
- Timm Maier 2 shared studies Solved some of the first cryo-EM structures of human mTORC1 (with Nenad Ban's group) and mTORC2, including a high-resolution map of mTORC2
- Alain Scaiola Structural biologist in Nenad Ban's group at ETH Zurich who solved the 3.2-angstrom cryo-EM structure of human mTORC2 and works on how ribosomes are built and how new proteins are processed
- Edward Stuttfeld Structural biologist who led the 2018 eLife study that gave the first detailed picture of the human mTORC2 core complex, working in Timm Maier's lab in Basel
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