Martin Walsh


Martin Walsh is Diamond's Life Sciences Coordinator, playing a role in management and development of life science research at Diamond, and sits on the eBIC Scientific Advisory Board. 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

Key Research Area

Other research activities

High-throughput methodologies for Macromolecular Crystallography
Cryo-Electron Microscopy

Latest Publications

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  1. Research
  2. Publications
  3. Collaborations
  4. Biography
Research -


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.



Publications - +

Publications since 2004

  1. C.D. Owen, P. Lukacik, J.A. Potter, O. Sleator, G.L. Taylor, M.A. Walsh, Streptococcus pneumoniae NanC: STRUCTURAL INSIGHTS INTO THE SPECIFICITY AND MECHANISM OF A SIALIDASE THAT PRODUCES A SIALIDASE INHIBITOR, J. Biol. Chem. 290 (2015) 27736–27748. doi:10.1074/jbc.M115.673632.
  2. D. L Caly, D. Bellini, M. A Walsh, J. Maxwell Dow, R. P Ryan, Targeting Cyclic di-GMP Signalling: A Strategy to Control Biofilm Formation? Curr. Pharm. Des. 21 (2015) 12–24.
  3. V. Arena de Souza, D.J. Scott, J.E. Nettleship, N. Rahman, M.H. Charlton, M.A. Walsh, et al., Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1, PLoS ONE. 10 (2015) e0143919. doi:10.1371/journal.pone.0143919.
  4. K. Adamczyk, N. Simpson, G.M. Greetham, A. Gumiero, M.A. Walsh, M. Towrie, et al., Ultrafast infrared spectroscopy reveals water-mediated coherent dynamics in an enzyme active site, Chemical Science. 6 (2015) 505–516.
  5. H.M. Ginn, G.K. Mostefaoui, K.E. Levik, J.M. Grimes, M.A. Walsh, A.W. Ashton, et al., SynchLink: an iOS app for ISPyB, J Appl Crystallogr. 47 (2014) 1781–1783. doi:10.1107/S1600576714017531.
  6. D. Bellini, D.L. Caly, Y. McCarthy, M. Bumann, S.-Q. An, J.M. Dow, 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 (2014) 26–38.[1]
  7. M. Candelaresi, A. Gumiero, K. Adamczyk, K. Robb, C. Bellota-Antón, V. Sangal, et al., A structural and dynamic investigation of the inhibition of catalase by nitric oxide, Org. Biomol. Chem. 11 (2013) 7778–7788. doi:10.1039/c3ob41977k.
  8. K. Adamczyk, M. Candelaresi, K. Robb, A. Gumiero, M.A. Walsh, A.W. Parker, et al., Measuring protein dynamics with ultrafast two-dimensional infrared spectroscopy, Measurement Science and Technology. 23 (2012) 062001.
  9. H. Gut, G. Xu, G.L. Taylor, M.A. Walsh, Structural basis for Streptococcus pneumoniae NanA inhibition by influenza antivirals zanamivir and oseltamivir carboxylate, J. Mol. Biol. 409 (2011) 496–503.
  10. L. Chen, S.W. Chan, X. Zhang, M. Walsh, C.J. Lim, W. Hong, et al., Structural basis of YAP recognition by TEAD4 in the hippo pathway, Genes \& Development. 24 (2010) 290–300.
  11. Gabadinho, J. et al. MxCuBE: a synchrotron beamline control environment customized for macromolecular crystallography experiments. Journal of Synchrotron Radiation 17, 700-707, doi:doi:10.1107/S0909049510020005 (2010).
  12. Cheng, Z. et al. Structural basis of the sensor-synthase interaction in autoinduction of the quorum sensing signal DSF biosynthesis. Structure 18, 1199-1209, doi:S0969-2126(10)00263-7 [pii] 10.1016/j.str.2010.06.011 (2010).
  13. Loh, P. G. et al. Structural basis for translational inhibition by the tumour suppressor Pdcd4. EMBO J 28, 274-285, doi:emboj2008278 [pii] 10.1038/emboj.2008.278 (2009).
  14. Flannery, D. et al. in Fifth IEEE Intnl. Conference on e-science. 201-207.
  15. Fang, F. et al. Allelic variation of bile salt hydrolase genes in Lactobacillus salivarius does not determine bile resistance levels. J Bacteriol 191, 5743-5757, doi:JB.00506-09 [pii] 10.1128/JB.00506-09 (2009).
  16. Rossi, F., Garavaglia, S., Montalbano, V., Walsh, M. A. & Rizzi, M. Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia. J Biol Chem 283, 3559-3566, doi:M707925200 [pii] 10.1074/jbc.M707925200 (2008).
  17. Oke, M. et al. Unusual chromophore and cross-links in ranasmurfin: a blue protein from the foam nests of a tropical frog. Angew Chem Int Ed Engl 47, 7853-7856, doi:10.1002/anie.200802901 (2008).
  18. Ling, S. H. et al. Crystal structure of human Edc3 and its functional implications. Mol Cell Biol 28, 5965-5976, doi:MCB.00761-08 [pii] 10.1128/MCB.00761-08 (2008).
  19. Gut, H., King, S. J. & Walsh, M. A. Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase. FEBS Lett 582, 3348-3352, doi:S0014-5793(08)00713-8 [pii] 10.1016/j.febslet.2008.08.026 (2008).
  20. Deshpande, A., Wang, S., Walsh, M. A. & Dokland, T. Structure of the equine arteritis virus nucleocapsid protein reveals a dimer-dimer arrangement. Acta Crystallographica Section D: Biological Crystallography 63, 581-586 (2007).
  21. Rosenbaum, G. et al. The Structural Biology Center 19ID undulator beamline: Facility specifications and protein crystallographic results. Journal of Synchrotron Radiation 13, 30-45 (2006).
  22. McMahon, S. A. et al. Crystallization of Ranasmurfin, a blue-coloured protein from Polypedates leucomystax. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 62, 1124-1126 (2006).
  23. Cipriani, F. et al. Automation of sample mounting for macromolecular crystallography. Acta Crystallographica Section D: Biological Crystallography 62, 1251-1259 (2006).
  24. Beteva, A. et al. High-throughput sample handling and data collection at synchrotrons: Embedding the ESRF into the high-throughput gene-to-structure pipeline. Acta Crystallographica Section D: Biological Crystallography 62, 1162-1169 (2006).
  25. Salgado, P. S., Walsh, M. A., Laurila, M. R. L., Stuart, D. I. & Grimes, J. M. Going soft and SAD with manganese. Acta Crystallographica Section D: Biological Crystallography 61, 108-111 (2005).
  26. Meier, C. et al. Overcoming the false-minima problem in direct methods: Structure determination of the packaging enzyme P4 from bacteriophage ?13. Acta Crystallographica Section D: Biological Crystallography 61, 1238-1244 (2005).
  27. Chen, N., Walsh, M. A., Liu, Y., Parker, R. & Song, H. Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping. Journal of Molecular Biology 347, 707-718 (2005).
  28. Van Den Heuvel, R. H. H. et al. Structural Studies on Flavin Reductase PheA2 Reveal Binding of NAD in an Unusual Folded Conformation and Support Novel Mechanism of Action. Journal of Biological Chemistry 279, 12860-12867 (2004).
  29. Sutton, G. et al. The nsp9 Replicase Protein of SARS-Coronavirus, Structure and Functional Insights. Structure 12, 341-353 (2004).
  30. Lo Surdo, P., Walsh, M. A. & Sollazzo, M. A novel ADP- and zinc-binding fold from function-directed in vitro evolution. Nature Structural and Molecular Biology 11, 382-383 (2004).
  31. Lartigue, A. et al. Sulfur Single-wavelength Anomalous Diffraction Crystal Structure of a Pheromone-Binding Protein from the Honeybee Apis mellifera L. Journal of Biological Chemistry 279, 4459-4464 (2004).
  32. Kong, C. et al. Crystal structure and functional analysis of the eukaryotic class II release factor eRF3 from S. pombe. Molecular Cell 14, 233-245 (2004).
  33. Kainov, D. E. et al. Crystallization and preliminary X-ray diffraction analysis of bacteriophage ?12 packaging factor P7. Acta Crystallographica Section D: Biological Crystallography 60, 2368-2370 (2004).
  34. Dottorini, T., Vaughan, C. K., Walsh, M. A., LoSurdo, P. & Sollazzo, M. Crystal Structure of a Human VH: Requirements for Maintaining a Monomeric Fragment. Biochemistry 43, 622-628 (2004).
  35. Dokland, T. et al. West Nile virus core protein: Tetramer structure and ribbon formation. Structure 12, 1157-1163 (2004).
Collaborations - +


University of Southampton
Prof Jeremy Webb and Dr. Ivo Tews

University of Strathclyde
Dr. Neil Hunt and Dr. Paul Hoskisson


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



Former Students:
Julie Thye, University of Durham
Victoria Arena, University of Oxford
Kirsty Robb, University of Strathclyde






Biography - +


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.