Martin Walsh


Martin Walsh is Deputy Director of Life Sciences at Diamond. Martin is also a Medical Research Council (MRC) funded Research Group Leader at the Research Complex at Harwell (RCaH). He joined Diamond in January 2009 from the MRC, France

Tel: +44 (0) 1235 778518

Techniques and Disciplines

Other Specialist Areas

  • Bacterial Respiratory Pathogens
  • High-throughput methodologies for Macromolecular Crystallography
  • Cryo-Electron microscopy.

Latest Publications

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Research Expertise

We are a structural biology group that uses primarily X-ray crystallography to determine macromolecular structures. In cases where we fail to obtain crystals we also utilise biological small angle scattering (BIOSAXS) and cryo-electron microscopy techniques. We complement our structural studies with a range of biochemical and spectroscopic techniques to fully understand the function and the dynamics of the systems under study.

Bacterial pathogenesis
Our research is using a targeted structural and functional approach to understanding at the molecular level how bacteria cause disease. We have focused our efforts in the main part on bacterial pathogens that continue to pose a significant health risk to the very young and elderly and have identified a number of vital processes within these pathogens to characterize and assess as targets for drug discovery. Our interests lie predominately in understanding the mechanisms used by bacterial pathogens to adhere to the host cell surfaces and the regulation of virulence. Presently we have several projects focused on understanding specific processes important to bacterial pathogenesis in three important human pathogens Streptococcus pneumoniae, Haemophilus influenzae and Pseudomonas aeruginosa.


Recent Publications

  1. Douangamath, A. et al. Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease. Nature Communications 11, 5047, (2020).
  2. Wu, H. et al. Fucosidases from the human gut symbiont Ruminococcus gnavus. Cell Mol Life Sci, (2020).
  3. Cai, Y. M. et al. Differential impact on motility and biofilm dispersal of closely related phosphodiesterases in Pseudomonas aeruginosa. Sci Rep 10, 6232, (2020).
  4. Bell, A. et al. Elucidation of a sialic acid metabolism pathway in mucus-foraging Ruminococcus gnavus unravels mechanisms of bacterial adaptation to the gut. Nat Microbiol 4, 2393-2404, (2019).
  5. Bartho, J. D. et al. The structure of Erwinia amylovora AvrRpt2 provides insight into protein maturation and induced resistance to fire blight by Malusxrobusta 5. J Struct Biol 206, 233-242, (2019).
  6. Salomone-Stagni, M. et al. A complete structural characterization of the desferrioxamine E biosynthetic pathway from the fire blight pathogen Erwinia amylovora. J Struct Biol 202, 236-249, (2018).
  7. Salomone-Stagni, M. et al. Structural and functional analysis of Erwinia amylovora SrlD. The first crystal structure of a sorbitol-6-phosphate 2-dehydrogenase. J Struct Biol 203, 109-119, (2018).
  8.  iNEXT Consortium: a European facility network to stimulate translational structural biology. FEBS Lett 592, 1909-1917, (2018).
  9. Grimes, J. M. et al. Where is crystallography going? Acta Crystallogr D Struct Biol 74, 152-166, (2018).
  10. Roversi, P. et al. Interdomain conformational flexibility underpins the activity of UGGT, the eukaryotic glycoprotein secretion checkpoint. Proc Natl Acad Sci U S A 114, 8544-8549, (2017).
  11. Culurgioni, S., Tang, M. & Walsh, M. A. Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092. Acta Crystallogr F Struct Biol Commun 73, 54-61, (2017).
  12. Culurgioni, S., Tang, M., Hall, D. R. & Walsh, M. A. Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092. J Vis Exp, (2017).
  13. Culurgioni, S., Harris, G., Singh, A. K., King, S. J. & Walsh, M. A. Structural Basis for Regulation and Specificity of Fructooligosaccharide Import in Streptococcus pneumoniae. Structure 25, 79-93, (2017).
  14. Clare, D. K. et al. Electron Bio-Imaging Centre (eBIC): the UK national research facility for biological electron microscopy. Acta Crystallogr D Struct Biol 73, 488-495, (2017).
  15. Bellini, D. et al. Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases. Sci Rep 7, 42166, (2017).
  16. Bartho, J. D. et al. The crystal structure of Erwinia amylovora AmyR, a member of the YbjN protein family, shows similarity to type III secretion chaperones but suggests different cellular functions. PLoS One 12, e0176049, (2017).
  17. Owen, C. D. et al. Streptococcus pneumoniae NanC: STRUCTURAL INSIGHTS INTO THE SPECIFICITY AND MECHANISM OF A SIALIDASE THAT PRODUCES A SIALIDASE INHIBITOR. J Biol Chem 290, 27736-27748, (2015).
  18. Lukacik, P. et al. High-resolution structures of Lactobacillus salivarius transketolase in the presence and absence of thiamine pyrophosphate. Acta Crystallogr F Struct Biol Commun 71, 1327-1334, (2015).
  19. Fisher, S. J., Levik, K. E., Williams, M. A., Ashton, A. W. & McAuley, K. E. SynchWeb: a modern interface for ISPyB. Journal of Applied Crystallography 48, 927-932, (2015).
  20. Caly, D. L., Bellini, D., Walsh, M. A., Dow, J. M. & Ryan, R. P. Targeting cyclic di-GMP signalling: a strategy to control biofilm formation? Curr Pharm Des 21, 12-24, (2015).
  21. Arena de Souza, V. et al. Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1. PLoS One 10, e0143919, (2015).
  22. Aller, P. et al. Application of in situ diffraction in high-throughput structure determination platforms. Methods Mol Biol 1261, 233-253, (2015).
  23. Adamczyk, K. et al. Ultrafast infrared spectroscopy reveals water-mediated coherent dynamics in an enzyme active site. Chemical Science 6, 505-516, (2015).
  24. Bellini, D. et al. Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre. Mol Microbiol 91, 26-38, (2014).


University of Southampton
Prof Jeremy Webb and Dr. Ivo Tew

Nationwide Childrens Hospital, Ohio USA

Dr. Sam King

Quadram Institute

Prof Nathalie Juge

University of Reading
Dr. Kim Watson and Dr. Sheila MacIntyre








After graduating from University College Galway (UCG) with a first class Honours degree in Chemistry in 1989, Walsh remained at UCG for his PhD work which used X-ray crystallography to fully characterize the flavoprotein, flavodoxin. This work aided in providing a general model for how flavoproteins modulate the redox potentials of flavin mononucleotide (FMN). The work was a significant milestone for structural biology in Ireland, as it presented the first protein crystal structures determined from an Irish-based research group.

Early postdoctoral work at York and EMBL Hamburg concentrated on the development and determination of protein structures at atomic resolution which was being pioneered at that time in Hamburg. This work contributed to introducing routine refinement of structures at this resolution as well as providing experimental data on the stereochemistry of amino acids in proteins.
In 1997 Walsh moved to Argonne National Laboratory (ANL) where he worked primarily on chaperonins and contributed to the commissioning of the world’s first dedicated insertion device beamline for exploiting anomalous diffraction in macromolecular crystallography: ID19 at the Advance Photon Source (APS). Work and associated research carried out at Argonne in the late 1990’s contributed strongly to establishing the MAD technique. In 1999 he moved to IRBM in Rome where work focused on the structural biology of the hepatitis C virus.
In 2001 he was appointed MRC group leader for BM14, based at the ESRF. Key hardware and software solutions to crystallography were delivered – automation of sample handling through robotics and management of crystallographic data (ISPyB) which have changed the way crystallographers now approach macromolecular structure determination at synchrotron beamlines.
In 2009, he joined Diamond Light Source with responsibility for life science research.

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