Google scholar:

Selected Research Papers:

Morris, K. L., Jones, J., Halebian, M., Wu, S., Baker, M., Armache, J., Ibarra, A. A., Session, R. B., Cameron, A. D., Cheng, Y., Smith, C. J., (2019). Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly. Nature Structural & Molecular Biology 26: 890-898.

EMDB-0126 PDB: 6SCT (triskelion hub consensus substructure)
EMDB-0114, 0115, 0116, 0118, 0120 (whole clathrin cage assemblies)
EMDB-0121, 0122, 0123, 0124, 0125 (triskelion hub substructure)
Whole clathrin cage assemblies models available upon request

Raw data:
EMPIAR-10294, 10295, 10296

Morris, K. L., Buffalo, C. Z., Stürzel, C. M., Heusinger, E., Kirchoff, F., Ren, X., Hurley, J. H. (2018). HIV-1 Nefs Are Cargo-Sensitive AP-1 Trimerization Switches in Tetherin Downregulation. Cell 174: 659-671.

EMDB-7457 PDB: 6CM9EMDB-7563 PDB: 6CRIEMDB-7455 PDB: 6DFFEMDB-7453 PDB: 6D84EMDB-7474 PDB: 6D83

Raw data:
EMPIAR-10178, 10177, 10176

The depicted Penrose triangle is a so-called impossible shape, however its 2-dimensional projection can still be realised by 3-dimensional models. Morris et al present the 3-dimensional structure of trimers, dimers and monomers of the vesicular coat protein adaptor assemblies AP-1:Arf1 hijacked by Nef and bound to the host antiviral protein tetherin, a trafficking cargo that is subjugated by HIV infection. The cryo-EM structures determined at high resolution describe the incredible diversity and seemingly impossibly complex landscape of AP-1 architectures that are assembled and allosterically controlled by Nef and cargo binding.

Su, M., Morris, K. L., Kim, D. J., Fu, Y., Lawrence, R., Stjepanovic, G., Zoncu, R., Hurley, J. H. (2017). Hybrid Structure of the RagA/C-Ragulator mTORC1 Activation Complex. Molecular Cell 68: 823-824. 

EMDB: 7072    PDB: 6B9X

Rapamycin was discovered in 1972 on the island of Rapa Nui, also known as Easter Island, in the Southern Pacific Ocean. Rapamycin is a potent inhibitor of the Mechanistic Target of Rapamycin 1 (mTORC1) kinase. Su et al report the structure of the RagA/C:Ragulator complex, which recruits mTORC1 to lysosomes, its site of activation. The RagA/C heads of this complex sit atop the Ragulator bodies that associate with the lysosomal surface, as if mimicking the monolithic heads (Moai) that decorate the landscape of Rapa Nui.

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

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 11, 1174.

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. & Adams, D. J. (2013). Chemically programmed self-sorting of gelator networks. Nature Communications 4, 1480.

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

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

Houton, K. A., Morris, K. L., Chen, L., Schmidtmann, M., Jones, J. T. A., Serpell, L. C., Lloyd, G. O. & Adams, D. J. (2012). On Crystal versus Fiber Formation in Dipeptide Hydrogelator Systems. Langmuir 28, 9797-806. 

Adams, D. J., Morris, K., Chen, L., Serpell, L. C., Bacsa, J. & Day, G. M. (2010). The delicate balance between gelation and crystallisation: structural and computational investigations. Soft Matter 6, 4144-56. 

Chen, L., Morris, K., Laybourn, A., Elias, D., Hicks, M. R., Rodger, A., Serpell, L. & Adams, D. J. (2010). Self-Assembly Mechanism for a Naphthalene-Dipeptide Leading to Hydrogelation. Langmuir 26, 5232-42. 

Collaborative Research Papers:

Horst, B. J., Yokom, A. L., Rosenberg, D. J., Morris, K. L., Hammel, M., Hurley, J. H., Marletta, M. A., (2019). Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy. eLife. 10.7554/eLife.50634.

Chang, C., Young, L. N., Morris, K. L., Bülow, S. V., 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. Molecular Cell 73(2): 339-353.

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. CrystEngComm 17(42): 8047-8057.

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.

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.

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

Xu, C., Liu, R., Mehta, A. K., Guerrero-Ferreira, R. C., Wright, E. R., Dunin-Horkawicz, S., Morris, K., 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. JACS 135(41): 15565-15578.

Pauwels, K., Williams, T. L., Morris, K. L., Jonckheere, W., Vandersteen, A., Kelly, G., Schymkowitz, J., Rousseau, F., Pastore, A., Serpell, L. C. & Broersen, K. (2012). Structural Basis for Increased Toxicity of Pathological Aß(42):Aß(40) Ratios in Alzheimer Disease. Journal of Biological Chemistry 287, 5650-60.

Marshall, K. E., Morris, K. L., Charlton, D., O’Reilly, N., Lewis, L., Walden, H. & Serpell, L. C. (2011). Hydrophobic, aromatic, and electrostatic interactions play a central role in amyloid fibril formation and stability. Biochemistry 50, 2061-71.

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

Liu, B., Moloney, A., Meehan, S., Morris, K., Thomas, S. E., Serpell, L. C., Hider, R., Marciniak, S. J., Lomas, D. A. & Crowther, D. C. (2010). Iron promotes the toxicity of amyloid-ß peptide by impeding its ordered aggregation. Journal of Biological Chemistry 286, 4248-56. 

Chen, L., Revel, S., Morris, K., Spiller, D. G., Serpell, L. C., Adams, D. J. (2010). Low molecular weight gelator-dextran composites. Chemical Communications 46, 6738-40. 

Chen, L., Revel, S., Morris, K., Serpell, L. C., Adams, D. J. (2010). Effect of Molecular Structure on the Properties of Naphthalene-Dipeptide Hydrogelators. Langmuir 26, 13466-71. 

Chen, L., Revel, S., Morris, K., Adams, D. J. (2010). Energy Transfer in Self-Assembled Dipeptide Hydrogels. Chemical Communications 46, 4267-69. 

Maurer-Stroh, S., Debulpaep, M., Kuemmerer, N., de la Paz, M. L., Martins, I. C., Reumers, J., Morris, K. L., Copland, A., Serpell, L., Serrano, L., Schymkowitz, J. W. & Rousseau, F. (2010). Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nature Methods 7, 237-42. 

Jahn, T. R., Makin, O. S., Morris, K. L., Marshall, K. E., Tian, P., Sikorski, P. & Serpell, L. C. (2009). The common architecture of cross-ß amyloid. Journal of Molecular Biology 395, 717-27. 


Morris, K., Serpell, L. C. (2010). From natural to designer self-assembling biopolymers, the structural characterisation of fibrous proteins & peptides using fibre diffraction. Chem Soc Rev 39, 3445-53. 

Book chapters:

Halebian, M., Morris, K. L. & Smith, C. J., (2017). Structure and Assembly of Clathrin Cages. Macromolecular Protein Complexes: Structure and Function (Harris, R. J. & Marles-Wright, J., ed.). Springer.

Morris, K. L. & Serpell, L. (2013). From molecular to supramolecular amyloid structures: contributions from fiber diffraction and electron microscopy. In Amyloid Fibrils and Prefibrillar Aggregates. Molecular and Biological Properties (Otzen, D. E., ed.). Viley-VCH, Aarhus, Denmark. 

Morris, K. L. & Serpell, L. C. (2012). X-Ray Fibre Diffraction Studies of Amyloid Fibrils. In Amyloid Proteins: Methods and Protocols, Vol. 849, pp. 121-135.