Dr Andrew Whitten
Role at ANSTO
Dr Andrew Whitten is an instrument scientist on the time-of-flight small-angle neutron scattering instrument BILBY time-of-flight small-angle neutron scattering instrument. He brings expertise in the area of small-angle scattering and neutron contrast variation from biological macromolecules. He has published widely in the area of low-resolution structure of proteins and protein complexes. His current primary research focus is on a class of proteins involved in trafficking vesicles to the cell membrane.
Dr Whitten undertook his PhD studies at the University of New England with Prof. Mark Spackman, where his research focused on the determination of the charge density distribution of molecular crystals using X-ray and neutron diffraction. Following this, Dr Whitten undertook a Post-Doctoral position at ANSTO working with Prof. Jill Trewhella, where he utilised small-angle scattering to study the structure of proteins involved in a range of biological processes. In 2009, Dr Whitten was awarded a prestigious NHMRC Peter Doherty Fellowship to work with Prof. Jenny Martin at the Institute for Molecular Bioscience at the University of Queensland. This research aimed to better understand the regulatory mechanisms of vesicle fusion through the use of a range of biophysical techniques including small-angle X-ray and neutron scattering.
Ph.D. in Chemistry, University of New England (2006)
Achievements and Affiliations
University Medal, University of New England (2001)
NHMRC Peter Doherty Fellow (2009-2012)
NHMRC Program Grant (Co-Investigator, 2009-2013)
NHMRC Project Grant (Chief Investigator B, 2014-2016)
Program Advisory Committee, Bragg Institute, ANSTO (2010)
Instrument Advisory Team, “Bilby – Time of flight small-angle neutron scattering instrument”, Bragg Institute, ANSTO (2010-)
Instrument Advisory Group, BioSAXS Beamline, Australian Synchrotron (2011-)
Scientific Program Committee, International Small-angle Scattering Conference (2012)
Australian Academy of Science National Committee for Crystallography (Young investigator, 2012-2013)
Royal Australian Chemical Institute, MRACI CChem (2001-)
Society of Crystallographers in Australia and New Zealand (2001-)
Adjunct Research Fellow, Institute for Molecular Bioscience, University of Queensland (2014-)
M. P. Christie, A. E. Whitten, G. J. King, S.-H. Hu, R. J. Jarrott, K.-E. Chen, A. P. Duff, P. Callow, B. M. Collins, D. E. James, J. L. Martin, 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. 109, 9816-9821 (2012).
G. J. King, J. Stockli, S.-H. Hu, B. Winnen, W. G. A. Duprez, C. C. Meoli, J. R. Junutula, R. J. Jarrott, D. E. James, A. E. Whitten, J. L. Martin, Membrane Curvature Protein Exhibits Interdomain Flexibility and Binds a Small GTPase, J. Biol. Chem. 287, 40996-41006 (2012).
A. E. Whitten, B. J. Smith, J. G. Menting, M. B. Margetts, N. M. McKern, G. O. Lovrecz, T. E. Adams, K. Richards, J. D. Bentley, J. Trewhella, C. W. Ward, M. C. Lawrence, Solution Structure of Ectodomains of the Insulin Receptor Family: The Ectodomain of the Type1 Insulin-Like Growth Factor Receptor Displays Asymmetry of Ligand Binding Accompanied by Limited Conformational Change, J. Mol. Biol. 394, 878-892 (2009).
A. E. Whitten, C. M. Jeffries, S. P. Harris, J. Trewhella, Cardiac myosin-binding protein C decorates F-actin: Implications for cardiac function, Proc. Natl. Acad. Sci. U.S.A. 105, 18360-18365 (2008).
A. E. Whitten, S. Cai, J. Trewhella, MULCh: ModULes for the analysis of small-angle neutron Contrast variation data from biomolecular assemblies, J. Appl. Crystallogr. 41, 222-226 (2008).
D. Comoletti, A. Grishaev, A. E. Whitten, I. Tsignelny, P. Taylor, J. Trewhella, Synaptic arrangement of the Neuroligin/&beta-Neurexin complex revealed by X-ray and neutron scattering, Structure. 15, 693-705 (2007).
A. E. Whitten, D. A. Jacques, B. Hammouda, T. Hanley, G. F. King, J. M. Guss, J. Trewhella, D. B. Langley, The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition, J. Mol. Biol. 368, 407-420 (2007).
A. E. Whitten, M. A. Spackman, Anisotropic displacement parameters for H atoms using an ONIOM approach, Acta Crystallogr. B62, 875-888 (2006).
A. E. Whitten, P. Turner, W. T. Klooster, R. O. Piltz, M. A. Spackman, Reassessment of large dipole moment enhancements in crystals: A detailed experimental and theoretical charge density analysis of 2-methyl-4-nitroaniline, J. Phys. Chem. A 110, 8763-8776 (2006).
A. E. Whitten, B. Dittrich, M. A. Spackman, P. Turner, T. C. Brown, Charge density analysis of two polymorphs of antimony(III) oxide, Dalton Trans. 1, 23-29 (2004).