Learn more about the group
We are part of the Division of Structural Biology at the Institute of Cancer Research in London.
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Research
Explore our research on nucleotide excision repair, the CDK-activating kinase, and high-resolution cryo-EM
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The Lab
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Publications
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News from the lab
Our paper on XPF-ERCC1 recruitment to SLX4-dependent DNA repair pathways has been published!December 16th, 2025
XPF-ERCC1 is a multifunctional DNA endonuclease. For Junjie's latest paper, we investigated how it is recruited to DNA repair pathways that depend on complex formation with SLX4. We discovered the mechanisms of XPF-ERCC1 recruitment and activation by SLX4, visualised a DNA-bound XPF-ERCC1-SLX4-SLX4IP complex, and more! Read the full story at Nature Communications. |
Now online: Structural basis of CDK recognition by the CDK-activating kinaseOctober 16th, 2025
Our paper on how the CDK-activating kinase recognises and activates other CDKs has now been published online. Throughout the course of this project, which was spearheaded by Victoria, we determined the structures of the human CAK in complex with CDK2, CDK2-cyclin A, CDK1-cyclin B, and CDK11. Based on this analysis, we derived the molecular mechanisms of substrate recognition by the CAK and proposed a model according to which this mechanisms applies to CAK-CDK complexes more generally. Read the full story at Science. |
New publication on CDK7 resistance to cancer therapeuticsSeptember 8th, 2025
For our most recent collaborative paper, Victoria determined the cryo-EM structure of a drug-resistant CDK7 mutant that the laboratory of Prof. Simak Ali (Imperial College London) discovered by in vitro evolution and then characterised in detail. Intriguingly, this mutant is resistant to reversible, high-affinity competitive inhibitors such as ICEC0942 and SY5609, but sensitive to covalent inhibitors. Read all about it at The EMBO Journal. |
New publication on cyclin docking motif discoveryAugust 15th, 2025
Our paper on high-throughput CDK-cyclin docking motif discovery, arising from a collaboration led by Dr. Norman Davey at the ICR, has now been published. We contributed the cryo-EM structures of three non-canonical docking peptides bound to CDK2-cyclin A, determined by Natàlia. Read all about it at Nature Communications. |
New publication on cryo-EM using a 100 kV microscopeJuly 30th, 2025
Our paper describing high-resolution structure determination of a wide range of macromolecular complexes - including the CDK-activating kinase - using the 100 kV Tundra cryogenic electron microscope has been published. This effort was spearheaded by Dr. Abhay Kotecha and colleagues at Thermo Fisher Scientific. Read all about it at Structure. |
Natàlia wins a short talk award!May 30th, 2025
Natàlia has won a short talk award at the workshop on "Machines acting on DNA and RNA, a molecular mechanistic perspective" at CNIO Madrid. She presented our latest findings on TFIIH activation during nucleotide excision repair. This comes after Victoria and Lucy won poster awards for their presentations at the BSG Winter Meeting at the MRC-LMB and the Chemistry Postgraduate Symposium at Imperial College, respectively. Well done everyone! |
New publication on CDK7 inhibition by SY5609February 28th, 2025
In collaboration with SYROS Pharmaceuticals, the groups of Prof. Dylan Taatjes and Prof. Robin Dowell (both CU Boulder), and Dr. Abhay Kotecha (Thermo Fisher Scientific), we have characterised the clinical CDK7 inhibitor SY-5609. Junjie determined cryo-EM structures of the human CAK bound to SY-5609 and SY-1365 to investigate the mechanisms of target specificity in these compounds. Data from our collaborators provide exciting new insights into the cellular functions of CDK7. Read all about it at Science Advances. |
Basil named EMBO Young InvestigatorDecember 3rd, 2024
Basil has been selected as one of twenty-seven young scientists to become EMBO Young Investigators from 2025-2028. Read more about it on the EMBO website. |
Review on high-resolution cryo-EM of small complexesApril 4th, 2024
Basil has written a review about high-resolution cryo-EM of small complexes and the application of these methods to the human CDK-activating kinase. Read all about it at Structure. |
Another new publication!March 13th, 2024
In collaboration with the groups of Prof. Simak Ali (Imperial College London) and Dr. Abhay Kotecha (Thermo Fisher Scientific), we established high-resolution/high-throughput cryo-EM workflows tailored for structure-based drug design. Applying these workflows to the ligand-bound human CDK-activating kinase, we determined more than a dozen structures at 2 Å resolution. Read all about it at Nature Communications. |
New publication!February 16th, 2024
In collaboration with the groups of Prof. Sandro Ataide (University of Sydney) and Dr. Abhay Kotecha (Thermo Fisher Scientific), Junjie determined the structure of the protein-binding domain of the SRP68/72 dimer, which forms part of the eukaryotic signal recognition particle. Read all about it at Nucleic Acids Research. |
New lab space & new lab membersAugust 23, 2021
We have moved into our newly refurbished lab space a few weeks ago (pictured on the left in its pristine state, though now already filled with lots of instruments and consumables). Junjie has joined the lab as a postdoc at the beginning of the month. Victoria (PhD student) and Natalia (postdoc) will join in the next few months. |
Structure of the CDK-activating kinase bound to ICEC0942January 19, 2021
Our latest paper reports the 2.5 Å-resolution structure of the CDK-activating kinase bound to the inhibitor ICEC0942 and has been published in the Biophysical Journal. This work was a collaboration with the laboratory of Prof. Simak Ali at Imperial College London and the data were collected during Basil's final days in the Nogales Lab in Berkeley. |
Structure of the human CDK-activating kinaseAugust 27, 2020
Basil's work on the structure of the CDK-activating kinase, performed in the Nogales Lab in Berkeley, has been published in PNAS. |