Senior Electron Microscope Scientist at the electron Bio-Imaging Centre (eBIC)
David joined eBIC in August 2020.
Email: [email protected]Tel: +44 (0) 1235 56 7521
Senior Electron Microscope Scientist at the electron Bio-Imaging Centre (eBIC)
David joined eBIC in August 2020.
Email: [email protected]David is a Senior Electron Microscope Scientist at the electron Bio-Imaging Centre (eBIC), Diamond Light Source. His research spans the breadth of structural biology, including X-ray crystallography, cryoEM and electron diffraction, with interests in both biological discovery and methods development.
After completing his PhD at the University of St Andrews in 2015, David joined Diamond's Macromolecular Crystallography group, where he investigated bacterial carbohydrate-processing systems and contributed to structure-based drug discovery efforts during the COVID-19 pandemic. These studies, particularly on membrane proteins recalcitrant to crystallisation, led to increasing use of cryoEM and ultimately a move to eBIC in 2020. He became a Senior Electron Microscope Scientist in 2025.
Although he retains a strong interest in understanding systems involved in carbohydrate recognition, transport and metabolism, David's current research is increasingly focused on developing new methods for protein electron diffraction (microED, 3DED, crED). He has a particular interest in applying lessons learned from decades of synchrotron macromolecular crystallography to electron diffraction, helping to accelerate the development of automated and high-throughput workflows. His work includes developing approaches for automated data processing and analysis, with the aim of making electron diffraction a more accessible and routine tool for structural biology.
David also leads eBIC's Chameleon user programme, supporting the use of an automated cryoEM sample preparation platform that enables rapid vitrification while reducing common grid-preparation artefacts such as preferred orientation, aggregation and air-water interface effects. He is interested in understanding how advances in sample preparation can improve specimen quality, reproducibility and throughput, and how these developments can be integrated with increasingly automated imaging and analysis workflows.
LE Tailford, CD Owen, J Walshaw, EH Crost, J Hardy-Goddard, G Le Gall, ... (2015) Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation Nature communications 6 (1), 1-12.
N Juge, L Tailford, CD Owen (2016) Sialidases from gut bacteria: a mini-review Biochemical Society Transactions 44 (1), 166-175.
CD Owen, P Lukacik, JA Potter, O Sleator, GL Taylor, MA Walsh (2015)
Streptococcus pneumoniae NanC Structural insights into the specificity and mechanism of a sialidase that produces a sialidase inhibitor Journal of Biological Chemistry 290 (46), 27736-27748.
CD Owen, LE Tailford, S Monaco, T Šuligoj, L Vaux, R Lallement, ... (2017) Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus Nature communications 8 (1), 1-15.
A Bell, J Brunt, E Crost, L Vaux, R Nepravishta, CD Owen, D Latousakis, ... (2019) Elucidation of a sialic acid metabolism pathway in mucus-foraging Ruminococcus gnavus unravels mechanisms of bacterial adaptation to the gut Nature microbiology 4 (12), 2393-2404.
LE Tailford, CD Owen, J Walshaw, EH Crost, J Hardy-Goddard, G Le Gall, ... (2015) Discovery of intramolecular trans-sialidases in human gut microbiota suggests novel mechanisms of mucosal adaptation. Nat Commun 6: 7624.
A Douangamath, D Fearon, P Gehrtz, T Krojer, P Lukacik, CD Owen, ... (2020) Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease bioRxiv.
H Wu, O Rebello, EH Crost, CD Owen, S Walpole, C Bennati-Granier, ... (2020) Fucosidases from the human gut symbiont Ruminococcus gnavus Cellular and Molecular Life Sciences, 1-19.
A Ronis, K Brockman, AK Singh, MO Gaytán, A Wong, S McGrath, ... (2019) Streptococcus oralis subsp. dentisani produces monolateral serine-rich repeat protein fibrils, one of which contributes to saliva binding via sialic acid Infection and immunity 87 (10), e00406-19.
CD Owen University of St Andrews (2015) Structural studies of non-classical sialidases.
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