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Home > Research Leaders > Emeritus > Tony Crowther
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Tony Crowther

Structure of macromolecule assemblies


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Tony Crowther’s first degree was in mathematics at Cambridge. After taking a postgraduate diploma in computing, he became a graduate student at the LMB. Most of his research career has been at the LMB, where he was Joint Head of the Structural Studies Division from 1994 to 2005.

In his early research he developed mathematical techniques for protein crystallography and for image processing in electron microscopy. His main research interests now are in virus structure and the abnormal filaments that form in neurodegenerative diseases. He is also still involved in development of computational methods for electron microscope imaging.

He is a Fellow of Peterhouse. He was elected a member of the European Molecular Biology Organisation in 1985, a Fellow of the Royal Society in 1993 and a Fellow of the Academy of Medical Sciences in 2007.


Our work aims to understand the structure of various macromolecular assemblies, particularly those involved in human disease. Electron microscopy of unstained samples in vitreous ice provides a way of visualizing such specimens, but direct interpretation is complicated because the image represents a low contrast projection of the specimen degraded by noise.

These difficulties can be overcome computationally by combining images of the specimen viewed from different angles and averaging using any inherent symmetry in the structure.

We solved the structure of hepatitis B virus core protein at 7.4Å resolution and recently proposed a model for the signalling of maturation of the core. Work on hepatitis B continues and we are trying to push the methods to higher resolution.

We are also investigating the structure of abnormal filaments which occur in the brain in Alzheimer’s and other neurodegenerative diseases, with a view to understanding their assembly and role in pathogenesis.

Selected Papers

  • Fitzpatrick AWP, Falcon B, He S, Murzin AG, Murshudov G, Garringer HJ, Crowther RA, Ghetti B, Goedert M, Scheres SHW (2017)
    CryoEM structures of tau filaments from Alzheimer’s disease
    Nature 547: 185-190.
  • Crowther RA (Volume editor) (2016)
    The Resolution Revolution: Recent Progress in CryoEM
    Methods in Enzymology 579: (Preface xiii-xx).
  • Roseman AM, Borschukova O, Berriman JA, Wynne SA, Pumpens P, Crowther RA. (2012)
    Structures of hepatitis B virus cores presenting a model epitope and their complexes with antibodies
    J Mol Biol. 423: 63-78

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