Dr. May Elizabeth Sharpe

Short description
Group Leader - MX Samples
May Sharpe
Paul Scherrer Institute PSI
Forschungsstrasse 111
5232 Villigen PSI


May Sharpe (neé Marsh) received her bachelor degree with First Class Honours in Biochemistry from the University of Sussex in 2004. In 2008 she completed her PhD at the University of Bristol in Structural Biology under the supervision of Dr. Andrea Hadfield. During her PhD she spent one year working at the Novartis Institute for Biomedical Research in Basel. In 2008 she moved to the University of Cambridge to join Professor Sir Tom Bundell's and Marko Hyvonen’s groups working as part of an inter-departmental Wellcome Trust seeded drug discovery initiative to develop protein-protein interaction inhibitors using fragment-based approaches. In 2012 she joined the Macromolecular Crystallography (MX) group as a post-doc working on the optical upgrade of the X06SA beam line. In 2013 she became the Crystallisation Facility Scientist responsible for setting up and running the PSI Crystallisation Facility, a joint facility of the PSD and BIO departments. Since 2018 she has been the Group Leader of the MX Samples group.

Responsibilities and Research

May leads the MX samples group, a subsection of the MX group responsible for protein crystal growth and sample delivery in support of macromolecular crystallography research at the SLS and SwissFEL. She also runs the PSI crystallisation facility, training users and overseeing the maintenance of crystallisation robotics and imagers. Finally, she shares responsibility for the Fast Fragment and Compound Screening (FFCS) pipeline together with Justyna Wojdyla. May’s scientific interests include protein crystallisation method development, particularly the use of seeding; fragment screening using X-ray crystallography, and the development of new methods for delivering crystallographic samples to the beam at synchrotron and XFEL beamlines.

  • Smith KML, Panepucci E, Kaminski JW, Aumonier S, Huang C-Y, Eris D, et al.
    SDU - software for high-throughput automated data collection at the Swiss Light Source
    Journal of Synchrotron Radiation. 2023; 30: 538-545. https://doi.org/10.1107/S1600577523002631
  • Stegmann DP, Steuber J, Fritz G, Wojdyla JA, Sharpe ME
    Fast fragment and compound screening pipeline at the Swiss Light Source
    In: Methods in enzymology. sine loco: Elsevier; 2023:235-284. https://doi.org/10.1016/bs.mie.2023.08.005
  • Huang C-Y, Aumonier S, Engilberge S, Eris D, Smith KML, Leonarski F, et al.
    Probing ligand binding of endothiapepsin by 'temperature-resolved' macromolecular crystallography
    Acta Crystallographica Section D: Structural Biology. 2022; 78: 964-974. https://doi.org/10.1107/S205979832200612X
  • Kaminski JW, Vera L, Stegmann DP, Vering J, Eris D, Smith KML, et al.
    Fast fragment- and compound-screening pipeline at the Swiss Light Source
    Acta Crystallographica Section D: Structural Biology. 2022; 78: 328-336. https://doi.org/10.1107/S2059798322000705
  • Mertens V, Abi Saad MJ, Coudevylle N, Wälti MA, Finke A, Marsh M, et al.
    Elucidation of a nutlin-derivative-HDM2 complex structure at the interaction site by NMR molecular replacement: a straightforward derivation
    Journal of Magnetic Resonance Open. 2022; 10-11: 100032 (5 pp.). https://doi.org/10.1016/j.jmro.2022.100032
  • Pedrini B, Finke AD, Marsh M, Luporini P, Vallesi A, Alimenti C
    Crystal structure of the pheromone Er-13 from the ciliate Euplotes raikovi, with implications for a protein-protein association model in pheromone/receptor interactions
    Journal of Structural Biology. 2022; 214(1): 107812 (10 pp.). https://doi.org/10.1016/j.jsb.2021.107812
  • Beale JH, Marsh ME
    Optimizing the growth of endothiapepsin crystals for serial crystallography experiments
    Journal of Visualized Experiments. 2021; 168: e61896 (30 pp.). https://doi.org/10.3791/61896
  • Martiel I, Beale JH, Karpik A, Huang C-Y, Vera L, Olieric N, et al.
    Versatile microporous polymer-based supports for serial macromolecular crystallography
    Acta Crystallographica Section D: Structural Biology. 2021; 77(9): 1153-1167. https://doi.org/10.1107/S2059798321007324
  • Mühlethaler T, Gioia D, Prota AE, Sharpe ME, Cavalli A, Steinmetz MO
    Comprehensive analysis of binding sites in tubulin
    Angewandte Chemie International Edition. 2021; 60(24): 13331-13342. https://doi.org/10.1002/anie.202100273
  • Ni X, Schröder M, Olieric V, Sharpe ME, Hernandez-Olmos V, Proschak E, et al.
    Structural insights into plasticity and discovery of remdesivir metabolite GS-441524 binding in SARS-CoV-2 macrodomain
    ACS Medicinal Chemistry Letters. 2021; 12(4): 603-609. https://doi.org/10.1021/acsmedchemlett.0c00684
  • Scott DE, Francis-Newton NJ, Marsh ME, Coyne AG, Fischer G, Moschetti T, et al.
    A small-molecule inhibitor of the BRCA2-RAD51 interaction modulates RAD51 assembly and potentiates DNA damage-induced cell death
    Cell Chemical Biology. 2021; 28(6): 835-847.e5. https://doi.org/10.1016/j.chembiol.2021.02.006
  • Sharpe ME, Wojdyla JA
    Fragment-screening and automation at the Swiss Light Source macromolecular crystallography beamlines
    Nihon Kessho Gakkaishi. 2021; 63(3): 232-235. https://doi.org/10.5940/jcrsj.63.232
  • Sutanto F, Shaabani S, Oerlemans R, Eris D, Patil P, Hadian M, et al.
    Combining high-throughput synthesis and high-throughput protein crystallography for accelerated hit identification
    Angewandte Chemie International Edition. 2021; 60(33): 18231-18239. https://doi.org/10.1002/anie.202105584
  • Bedi RK, Huang D, Wiedmer L, Li Y, Dolbois A, Wojdyla JA, et al.
    Selectively disrupting m6A-dependent protein-RNA interactions with fragments
    ACS Chemical Biology. 2020; 15(3): 618-625. https://doi.org/10.1021/acschembio.9b00894
  • Nass K, Cheng R, Vera L, Mozzanica A, Redford S, Ozerov D, et al.
    Advances in long-wavelength native phasing at X-ray free-electron lasers
    IUCrJ. 2020; 7: 965-975. https://doi.org/10.1107/S2052252520011379
  • Opara NL, Mohacsi I, Makita M, Castano-Diez D, Diaz A, Juranić P, et al.
    Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals
    Structural Dynamics. 2018; 5(5): 054303 (15 pp.). https://doi.org/10.1063/1.5050618
  • Sommer R, Makshakova ON, Wohlschlager T, Hutin S, Marsh M, Titz A, et al.
    Crystal structures of fungal tectonin in complex with O-methylated glycans suggest key role in innate immune defense
    Structure. 2018; 26(3): 391-402. https://doi.org/10.1016/j.str.2018.01.003
  • Weinert T, Olieric N, Cheng R, Brünle S, James D, Ozerov D, et al.
    Serial millisecond crystallography for routine room-temperature structure determination at synchrotrons
    Nature Communications. 2017; 8(1): 542 (11 pp.). https://doi.org/10.1038/s41467-017-00630-4
  • Chatterjee A, Mallin H, Klehr J, Vallapurackal J, Finke AD, Vera L, et al.
    An enantioselective artificial Suzukiase based on the biotin-streptavidin technology
    Chemical Science. 2016; 7(1): 673-677. https://doi.org/10.1039/c5sc03116h
  • Marsh ME, Scott DE, Ehebauer MT, Abell C, Blundell TL, Hyvönen M
    ATP half-sites in RadA and RAD51 recombinases bind nucleotides
    FEBS Open Bio. 2016; 6(5): 372-385. https://doi.org/10.1002/2211-5463.12052
  • Moschetti T, Sharpe T, Fischer G, Marsh ME, Ng HK, Morgan M, et al.
    Engineering archeal surrogate systems for the development of protein-protein interaction inhibitors against human RAD51
    Journal of Molecular Biology. 2016; 428(23): 4589-4607. https://doi.org/10.1016/j.jmb.2016.10.009
  • Orts J, Wälti MA, Marsh M, Vera L, Gossert AD, Güntert P, et al.
    NMR-based determination of the 3D structure of the ligand-protein interaction site without protein resonance assignment
    Journal of the American Chemical Society. 2016; 138(13): 4393-4400. https://doi.org/10.1021/jacs.5b12391
  • Scott DE, Marsh M, Blundell TL, Abell C, Hyvönen M
    Structure-activity relationship of the peptide binding-motif mediating the BRCA2:RAD51 protein-protein interaction
    FEBS Letters. 2016; 590(8): 1094-1102. https://doi.org/10.1002/1873-3468.12139
  • Campagne S, Marsh ME, Capitani G, Vorholt JA, Allain FH-T
    Structural basis for -10 promoter element melting by environmentally induced sigma factors
    Nature Structural and Molecular Biology. 2014; 21(3): 269-276. https://doi.org/10.1038/nsmb.2777
  • D'Arcy A, Bergfors T, Cowan-Jacob SW, Marsh M
    Microseed matrix screening for optimization in protein crystallization: what have we learned?
    Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2014; 70(9): 1117-1126. https://doi.org/10.1107/S2053230X14015507
  • Prota AE, Bargsten K, Diaz JF, Marsh M, Cuevas C, Liniger M, et al.
    A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs
    Proceedings of the National Academy of Sciences of the United States of America PNAS. 2014; 111(38): 13817-13821. https://doi.org/10.1073/pnas.1408124111
  • Prota AE, Bargsten K, Northcote PT, Marsh M, Altmann K-H, Miller JH, et al.
    Structural basis of microtubule stabilization by laulimalide and peloruside A
    Angewandte Chemie International Edition. 2014; 53(6): 1621-1625. https://doi.org/10.1002/anie.201307749
  • Gao Y, Ran T, Marsh M, Zhu W, Wang M, Mao X, et al.
    Crystal structures of Cg1458 reveal a catalytic lid domain and a common catalytic mechanism for the FAH family
    Biochemical Journal. 2013; 449(1): 51-60. https://doi.org/10.1042/BJ20120913
  • Scott DE, Ehebauer MT, Pukala T, Marsh M, Blundell TL, Venkitaraman AR, et al.
    Using a fragment-based approach to target protein-protein interactions
    ChemBioChem. 2013; 14(3): 332-342. https://doi.org/10.1002/cbic.201200521