Kyle Morris

Kyle obtained his Ph.D. from the University of Sussex (Serpell lab: 2008-2012) where he used biophysics, scattering and electron microscopy (EM) to model the structures of fibrillar self-assemblies. Kyle continued to work in protein self-assembly at the University of Warwick (Smith lab: 2013-2016) and then the University of California Berkeley (Hurley lab: 2016-2018). During his post-doctoral training, he also had the opportunity to train in the Cheng lab at UCSF.

In the Smith lab, Kyle determined the structures of five unique architectures of the coat protein clathrin. At the time, this work presented the highest resolution description of the core assembly structure of this complex. Clathrin is involved in coordinating protein trafficking in cells and their structure provided insight into the assembly’s inherent adaptability during membrane encapsulation of cargos. The data were collected at several facilities worldwide and Kyle was fortunate to gain insight into how different facilities operated. In the Hurley lab, Kyle determined the structure of the related trafficking protein, the AP-1 trimer, in complex with HIV Nef and the antiviral protein tetherin. The structure revealed a potential mechanism by which an HIV protein could subvert trafficking of an antiviral protein, such that viral infection can progress. The study also proposes why pandemic strains of HIV have evolved differing strategies of tetherin restriction.

Kyle returned to the UK to the MRC London Institute of Medical Sciences as a Senior Investigator Scientist (2018-2021), joining the team developing the EM capabilities of the institute. He worked on projects related to gene editing, genomic maintenance, epigenetics and became interested in using EM for cellular and correlative imaging. In partnership with Material Sciences (Imperial), he developed FIB-SEM workflows and built collaborations between cell biologists and electron microscopists. Kyle led the award and installation of a new facility housing a Talos TEM, GP2 plunger, automatic serial block face SEM, and instrumentation for array tomography and cryo-CLEM.

Kyle works to unite his scientific interests, with technology development and a passion for enabling scientists to access cryo-EM for their research. He joined the eBIC team at the Diamond Light Source in 2021 as a senior EM scientist and training co-ordinator.

Gutierrez-Escribano, P., Hormeño, S., Madariaga-Marcos, J., Solé-Soler, R., O'Reilly, F., Morris, K. L., Aicart-Ramos, C., Aramayo, R., Montoya, A., Kramer, H., Rappsilber, J., Torres-Rosell, J., Moreno-Herrero, F., and Aragon, L., (2020). Purified Smc5/6 complex exhibits DNA substrate recognition and compaction Mol Cell 80:1039-1054

Turnbull, R., Fairall, L., Saleh, A., Kelsall, E., Morris, K. L., Ragan, T., Savva, C., Chandru, A., Millard, C., Makarova, O., Smith, C. J., Roseman, A., Fry, A., Cowley, S. and Schwabe, J. W. R., (2020). The MiDAC histone deacetylase complex is essential for embryonic development and has a unique multivalent structure. Nat Comm 11:3252

Morris, K. L., Jones, J. R., Halebian, M., Wu, S., Baker, M., Armache, J. P., Avila Ibarra, A., Sessions, R. B., Cameron, A. D., Cheng, Y. and Smith, C. J. (2019). Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly. Nat Struct Mol Biol 26(10): 890-898.

Horst, B. G., Yokom, A. L., Rosenberg, D. J., Morris, K. L., Hammel, M., Hurley, J. H. and Marletta, M. A. (2019). Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy. eLife 8: e50634.

Chang, C., Young, L. N., Morris, K. L., von Bülow, S., Schöneberg, J., Yamamoto-Imoto, H., Oe, Y., Yamamoto, K., Nakamura, S., Stjepanovic, G., Hummer, G., Yoshimori, T. and Hurley, J. H. (2019). Bidirectional Control of Autophagy by BECN1 BARA Domain Dynamics. Mol Cell 73(2): 339-353.e336.

Morris, K. L., Buffalo, C. Z., Stürzel, C. M., Heusinger, E., Kirchhoff, F., Ren, X. and Hurley, J. H. (2018). HIV-1 Nefs are cargo-sensitive AP-1 trimerization switches in tetherin downregulation. Cell (3): 659-671.e614.

Su, M.-Y., Morris, K. L., Kim, D. J., Fu, Y., Lawrence, R., Stjepanovic, G., Zoncu, R. and Hurley, J. H. (2017). Hybrid Structure of the RagA/C-Ragulator mTORC1 Activation Complex. Mol Cell 68(5): 835-846.e833.

Millard, C. J., Varma, N., Saleh, A., Morris, K. L., Watson, P. J., Bottrill, A. R., Fairall, L., Smith, C. J. and Schwabe, J. W. R. (2016). The structure of the core NuRD repression complex provides insights into its interaction with chromatin. eLife 5: e13941.

Al-Garawi, Z. S., Morris, K. L., Marshall, K. E., Eichler, J. and Serpell, L. C. (2017). The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides. Interface Focus 7(6): 20170027.

Langkilde, A. E., Morris, K. L., Serpell, L. C., Svergun, D. I. and Vestergaard, B. (2015). The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy. Acta Crystallogr D Biol Crystallogr 71(Pt 4): 882-895.

Draper, E. R., Morris, K. L., Little, M. A., Raeburn, J., Colquhoun, C., Cross, E. R., McDonald, T. O., Serpell, L. C. and Adams, D. J. (2015). Hydrogels formed from Fmoc amino acids. Cryst Eng Comm 17(42): 8047-8057.

Morris, K. L., Chen, L., Rodger, A., Adams, D. J. and Serpell, L. C. (2015). Structural determinants in a library of low molecular weight gelators. Soft Matter.

Colquhoun, C., Draper, E. R., Eden, E. G. B., Cattoz, B. N., Morris, K. L., Chen, L., McDonald, T. O., Terry, A. E., Griffiths, P. C., Serpell, L. C. and Adams, D. J. (2014). The effect of self-sorting and co-assembly on the mechanical properties of low molecular weight hydrogels. Nanoscale 6(22): 13719-13725.

Morris, K. L., Chen, L., Raeburn, J., Sellick, O. R., Cotanda, P., Paul, A., Griffiths, P. C., King. S. M., O'Reilly, R. K., Serpell, L. C. and Adams, D. J. (2013). Chemically programmed self-sorting of gelator networks. Nat Comm 4: 1480.

Xu, C., Liu, R., Mehta, A. K., Guerrero-Ferreira, R. C., Wright, E. R., Dunin-Horkawicz, S., Morris, K. L., Serpell, L. C., Zuo, X., Wall, J. S. and Conticello, V. P. (2013). Rational Design of Helical Nanotubes from Self-Assembly of Coiled-Coil Lock Washers. Journal of the American Chemical Society 135(41): 15565-15578.

Morris, K. L., Rodger, A., Hicks, M. R., Debulpaep, M., Schymkowitz, J., Rousseau, F. and Serpell, L. C. (2013). Exploring the sequence-structure relationship for amyloid peptides. Biochem J 450(2): 275-283.

Morris, K. L., Zibaee, S., Chen, L., Goedert, M., Sikorski, P. and Serpell, L. C. (2013). The Structure of Cross-β Tapes and Tubes Formed by an Octapeptide, αSβ1. Angewandte Chemie International Edition 52(8): 2279-2283.

Al-Hilaly, Y., T. Williams, M. Stewart-Parker, L. Ford, E. Skaria, M. Cole, W. Bucher, K. L. Morris, A. Sada, J. Thorpe and L. Serpell (2013). A central role for dityrosine crosslinking of Amyloid-beta in Alzheimer's disease. Acta Neuropathologica Communications 1(1): 83.

Houton, K. A., Morris, K. L., Chen, L., Schmidtmann, M., Jones, J. T. A., Serpell, L. C., Lloyd, G. O. and Adams, D. J. (2012). On Crystal versus Fiber Formation in Dipeptide Hydrogelator Systems. Langmuir 28(25): 9797-9806.

Pauwels, K., Williams, T. L., Morris, K. L., Jonckheere, W., Vandersteen, A., Kelly, G., Schymkowitz, J., Rousseau, F., Pastore, A., Serpell, L. C. and Broersen, K. (2012). Structural Basis for Increased Toxicity of Pathological Aß(42):Aß(40) Ratios in Alzheimer Disease. JBC 287(8): 5650-5660.

Liu, B., Moloney, A., Meehan, S., Morris, K. L., Thomas, S. E., Serpell, L. C., Hider, R., Marciniak, S. J., Lomas, D. A. and Crowther, D. C. (2011). Iron Promotes the Toxicity of Amyloid ß Peptide by Impeding Its Ordered Aggregation. JBC 286(6): 4248-4256.

Chen, L., Pont, G., Morris, K. L., Lotze, G., Squires, A., Serpell, L. C. and Adams, D. J. (2011). Salt-induced hydrogelation of functionalised-dipeptides at high pH. Chem Comm 47(44): 12071-12073.

Marshall, K. E., Morris, K. L., Charlton, D., O'Reilly, N., Lewis, L., Walden, H.  and Serpell, L. C. (2011). Hydrophobic, Aromatic, and Electrostatic Interactions Play a Central Role in Amyloid Fibril Formation and Stability. Biochemistry 50(12): 2061-2071.

Adams, D. J., Morris, K. L., Chen, L., Serpell, L. C., Bacsa, J. and Day, G. M. (2010). The delicate balance between gelation and crystallisation: structural and computational investigations. Soft Matter 6(17): 4144-4156.

Maurer-Stroh, S., Debulpaep, M., Kuemmerer, N., de la Paz, M. L., Martins, I. C., Reumers, J., Morris, K. L., Copland, A., Serpell, L. C., Serrano, L., Schymkowitz, J. W. H. and Rousseau, F. (2010). Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nature Methods 7(3): 237-242.

Chen, L., Morris, K. L., Laybourn, A., Elias, D., Hicks, M. R., Rodger, A., Serpell, L. C. and Adams, D. J. (2010). Self-Assembly Mechanism for a Naphthalene-Dipeptide Leading to Hydrogelation. Langmuir 26(7): 5232-5242.

Chen, L., Revel, S., Morris, K. L., Serpell, L. C. and Adams, D. J. (2010). Effect of Molecular Structure on the Properties of Naphthalene-Dipeptide Hydrogelators. Langmuir 26(16): 13466-13471.

Chen, L., Revel, S., Morris, K. L. and Adams, D. J. (2010). Energy transfer in self-assembled dipeptide hydrogels. Chem Comm 46(24): 4267-4269.

Chen, L., Revel, S., Morris, K. L., Spiller, D. G., Serpell, L. C. and Adams, D. J.  (2010). Low molecular weight gelator-dextran composites. Chem Comm 46(36): 6738-6740.

Jahn, T. R., Makin, O. S., Morris, K. L., Marshall, K. E., Tian, P., Sikorski, P. and Serpell, L. C. (2010). The Common Architecture of Cross-ß Amyloid. JMB 395(4): 717-727.