Dr Anthony Duff

Structural Biologist
Phone - +61 2 9717 3493
Anthony Duff 180x180px


Role at ANSTO

Anthony Duff is a structural biologist interested in the structure and function of biological macromolecules. Ultimately, the goal is to understand the mechanism of life at the molecular level. The field of structural biology is inherently an interdisciplinary and collaborative science involving a range of complementary methods.

Prominent examples are X-ray crystallography and nuclear magnetic resonance spectroscopy, which provide precise information on rigid biomolecular structures, and electron microscopy which provides moderate resolution structural information on large assemblies, including membrane structures. To complement these structural techniques, we aim to use small-angle X-ray and neutron scattering to characterise the dynamic structures of biological macromolecular assemblies.


Qualifications & Achievements


  • Ph.D. from the School of Physics, The University of New South Wales, submitted 1999

Title:  Crystallographic Studies of the Protein Rubisco: New Perspectives on Closure and Catalysis in this Two-State Metalloenzyme
Supervisor:     Dr Paul M.G. Curmi, Protein Structure Group.
Co-supervisor:    Prof. T. John Andrews, ANU

  • B.Sc.(Hons) majoring in physics, from The University of New South Wales, 1993
  • Graduate Certificate in Adult Education, from The University of New England, 2008

Selected publications

Robust High-Yield Methodologies for 2H and 2H/15N/13C Labeling of Proteins for Structural Investigations Using Neutron Scattering and NMR, Methods in Enzymology, Available online 21 July 2015
Anthony P. Duff, Karyn L. Wilde, Agata Rekas, Vanessa Lake, Peter J. Holden, Production and characterization of recombinant perdeuterated cholesterol oxidase
Analytical Biochemistry (2015) 485 102-108
Emily Golden, Paul V Attwood, Anthony P. Duff, Flora Meilleur; Alice Vrielink, Structure of GUN4 from Chlamydomonas reinhardtii Acta Crystallographica Section F (2015) 71 1094-1099
Shabnam Tarahi Tabrizi), David B. Langley; Stephen J. Harrop, Anthony P. Duff, Robert D. Willows, Structural and functional consequences of succinate dehydrogenase subunit B mutations, Endocrine-Related Cancer (2015) 22(3) 387-397
E Kim, E M Rath, V H M Tsang, A P Duff, B G Robinson, W B Church, D E Benn, T Dwight, and R J Clifton-Bligh, Differential ultracentrifugation coupled to small angle X-ray scattering on macromolecular complexes, J. Appl. Cryst. (2015). 48, 769–775
Robert M. G. Hynson, Anthony P. Duff, Nigel Kirby, Stephan Mudie and Lawrence K. Lee, Small-angle X-ray scattering of BAMLET at pH 12: A complex of alpha-lactalbumin and oleic acid Proteins – Structure Function and bioinformatics (2014) 82 (7), 1400-1408
Emma M. Rath, Anthony P. Duff, Anders P. Hakansson, Robert B. Knott, and W. Bret Church, CLIC proteins, ezrin, radixin, moesin and the coupling of membranes to the actin cytoskeleton: A smoking gun?  Biochim Biophys Acta (2014) 1838 (2) 643-657  
Jiang, L., Phang, J. M., Yu, J., Harrop, S. J., Sokolova, A. V., Duff, A. P., Wilk, K. E., Alkhamici, H., Breit, S. N., Valenzuela, S. M., Brown, L. J., and Curmi, P. M.
Correlation of thermostability and conformational changes of catechol 2, 3-dioxygenases from two disparate micro-organisms. Biophysical Chemistry (2013) 180, 145-152
Sokolova, A., Huang, S.-L., Duff, A., Gilbert, E. P., and Li, W.-H. Targeted detection of phosphatidylserine in biomimetic membranes and in vitro cell systems using annexin V-containing cubosomes. Biomaterials (2013) 34, 8361-8369
Shen, H. H., Lake, V., Le Brun, A. P., James, M., Duff, A. P., Peng, Y., McLean, K. M., and Hartley, P. G. Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release. Biophysical Journal (2012) 103, 541-549 
Taylor, J. E., Chow, J. Y., Jeffries, C. M., Kwan, A. H., Duff, A. P., Hamilton, W. A., and Trewhella, J. Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity. Angewandte Chemie International Edition  (2012) 51, 12621-12625 
Morris, V. K., Linser, R., Wilde, K. L., Duff, A. P., Sunde, M., and Kwan, A. H. Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide.   Proc. Natl. Acad. Sci. U. S. A. (2012) 109, 9816-9821 
Christie, M. P., Whitten, A. E., King, G. J., Hu, S.-H., Jarrott, R. J., Chen, K.-E., Duff, A. P., Callow, P., Collins, B. M., James, D. E., and Martin, J. L. High yield expression and efficient purification of deuterated human protein galectin-2. Food and Bioproducts Processing (2012) 90, 563-572 
Chen, X., Wilde, K. L., Wang, H., Lake, V., Holden, P. J., Middelberg, A. P. J., He, L., and Duff, A. P. Complexes of the copper-containing amine oxidase from Arthrobacter globiformis with the inhibitors benzylhydrazine and tranylcypromine. Acta Crystallogr. F-Struct. Biol. Cryst. Commun. (2008) 64, 577-583 
Langley, D. B., Trambaiolo, D. M., Duff, A. P., Dooley, D. M., Freeman, H. C., and Guss, J. M. Enantiomer-specific binding of ruthenium(II) molecular wires by the amine oxidase of Arthrobacter globiformis. J. Am. Chem. Soc. (2008) 130, 8069-8078 
Langley, D. B., Brown, D. E., Cheruzel, L. E., Contakes, S. M., Duff, A. P., Hilmer, K. M., Dooley, D. M., Gray, H. B., Guss, J. M., and Freeman, H. C. The copper-containing amine oxidase from Arthrobacter globiformis: refinement at 1.55 and 2.20 angstrom resolution in two crystal forms. Acta Crystallogr. F-Struct. Biol. Cryst. Commun. (2006) 62, 1052-1057 
Langley, D. B., Duff, A. P., Freeman, H. C., and Guss, J. M. A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer.  Acta Crystallogr. F-Struct. Biol. Cryst. Commun. (2006) 62, 1168-1173 
Duff, A. P., Shepard, E. M., Langley, D. B., Dooley, D. M., Freeman, H. C., and Guss, J. M. The 1.23 angstrom structure of Pichia pastoris lysyl oxidase reveals a lysine-lysine cross-link.  Acta Crystallogr. Sect. D-Biol. Crystallogr. (2006) 62, 1073-1084 
Duff, A. P., Cohen, A. E., Ellis, P. J., Hilmer, K., Langley, D. B., Dooley, D. M., Freeman, H. C., and Guss, J. M. Crystal structures of recombinant human purple acid phosphatase with and without an inhibitory conformation of the repression loop. J. Mol. Biol. (2005)351, 233-246 
Strater, N., Jasper, B., Scholte, M., Krebs, B., Duff, A. P., Langley, D. B., Han, R. L., Averill, B. A., Freeman, H. C., and Guss, J. M. Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires. Proc. Natl. Acad. Sci. U. S. A. (2005) 102, 13451-13456 
Contakes, S. M., Juda, G. A., Langley, D. B., Halpern-Manners, N. W., Duff, A. P., Dunn, A. R., Gray, H. B., Dooley, D. M., Guss, J. M., and Freeman, H. C.
Differential inhibition of six copper amine oxidases by a family of 4-(aryloxy)-2-butynamines: Evidence for a new mode of inactivation.  Biochemistry (2004) 43, 10965-10978  
O'Connell, K. M., Langley, D. B., Shepard, E. M., Duff, A. P., Jeon, H. B., Sun, G., Freeman, H. C., Guss, J. M., Sayre, L. M., and Dooley, D. M. Using xenon as a probe for dioxygen-binding sites in copper amine oxidases.  J. Mol. Biol. (2004) 344, 599-607 
Duff, A. P., Trambaiolo, D. M., Cohen, A. E., Ellis, P. J., Juda, G. A., Shepard, E. M., Langley, D. B., Dooley, D. M., Freeman, H. C., and Guss, J. M. New crystallographic studies of copper amine oxidases. Journal of Inorganic Biochemistry J. Inorg. Biochem. (2003)96, 132-132
Freeman, H. C., Cohen, A., Dooley, D. M., Duff, A. P., Ellis, P. J., Guss, J. M., Langley, D. B., and Trambaiolo, D. M. The crystal structure of Pichia pastoris lysyl oxidase. Biochemistry (2003) 42, 15148-15157 
Duff, A. P., Cohen, A. E., Ellis, P. J., Kuchar, J. A., Langley, D. B., Shepard, E. M., Dooley, D. M., Freeman, H. C., and Guss, J. M. The transition between the open and closed states of rubisco is triggered by the inter-phosphate distance of the bound bisphosphate. J. Mol. Biol. (2000) 298, 903-916