Dr Ben Hankamer
Affiliation: Institute for Molecular Bioscience, University of Queensland
Queensland Bioscience Precinct
306 Carmody Rd
The University of Queensland
Phone: +61 (07) 3346 2100
Fax: +61 (07) 3346 2101
Our group is focused on developing a broad based platform for the structure determination of membrane proteins and macromolecular assemblies, based upon single particle analysis, electron and X-ray crystallography.
A strong research focus of the group is on automation to increase the rate of protein structure determination. A selection of proteins involved in a range of important biological processes and biotechnology applications (eg. Biohydrogen) are currently being investigated as part of the IMB's Visual Cell program.
Single Particle analysis
Single particle analysis (SPA), when coupled with electron cryo-microscopy, is ideally suited for the structure determination of large membrane proteins and macromolecular assemblies.In essence, SPA is the process of determining 3D reconstructions of macromolecules from their constituent 2D projection images captured by electron cryo-microscopy.
- Electron Crystallography
Electron crystallography requires the use of 2D crystals. These are particularly well suited for membrane protein structure determination as the crystallized proteins are arrayed within a near native lipid bilayer.
The 2D crystals are imaged over a range of tilt angles and the processed images merged to facilitate 3D image reconstruction. New processes of monolayer and bilayer crystallogenesis methods are being developed to facilitate template mediated crystal production.
- Cubic Phase crystallization
The use of cubic phase lipids for the purpose of membrane protein crystallization is also being explored. Cubic phase lipid structures are highly ordered, contorted bilayers, which are continuous and organized in 3D space.
Membrane proteins can be inserted into these cubic phase lipid matrices and induced to form highly ordered three-dimensional crystals well suited for high resolution X-ray crystallographic analysis. The method can be thought of as a hybrid between 2D bilayer and 3D crystal production.
Biology and Biotechnology
The development of a clean, sustainable and economically viable energy supply for the future is one of the most urgent challenges of our generation, given that oil production is estimated to peak in 5-33 years time.
There is now a concerted international effort to switch from a fossil fuel to a hydrogen economy. We are exploring the use of a green algal system that uses solar energy to split water (H2O) into hydrogen (H2) and oxygen (O2), for large scale H2 production. Subsequent combustion of H2 yields only H2O eliminating both net H2O use and the production of harmful greenhouse gases, associated with the burning of fossil fuels.
The identification of marine algae capable of producing H2 has the added benefit that H2 production could be coupled with H2O purification, as the product of H2 combustion is pure H2O.
- Hankamer BD, Elderkin SL, Buck M, Nield J. Organisation of the AAA+ adaptor protein PspA: an oligomeric ring. J Biol Chem. 2003 Dec 19
- Iwata M, Imamura H, Stambouli E, Ikeda C, Tamakoshi M, Nagata K, Makyio H, Hankamer B, Barber J, Yoshida M, Yokoyama K, Iwata S. Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase.Proc Natl Acad Sci U S A. 2004 Jan 6; 101(1): 59-64.
- Sennoga C, Heron A, Seddon JM, Templer RH, Hankamer B. Membrane-protein crystallization in cubo: temperature-dependent phase behaviour of monoolein-detergent mixtures. Acta Crystallogr D Biol Crystallogr. 2003 Feb; 59(Pt 2): 239-46.
- da Fonseca P, Morris EP, Hankamer B, Barber J. Electron crystallographic study of photosystem II of the cyanobacterium
Synechococcus elongatus. Biochemistry. 2002 Apr 23; 41(16): 5163-7.
- Hankamer B, Morris E, Nield J, Gerle C, Barber J. Three-dimensional structure of the photosystem II core dimer of higher plants determined by electron microscopy.
J Struct Biol. 2001 Sep; 135(3): 262-9.
- Hankamer B, Morris E, Nield J, Carne A, Barber J. Subunit positioning and transmembrane helix organisation in the core dimer of
photosystem II. FEBS Lett. 2001 Aug 31; 504(3): 142-51. Review.
- Barter LM, Bianchietti M, Jeans C, Schilstra MJ, Hankamer B, Diner BA,
Barber J, Durrant JR, Klug DR. Relationship between excitation energy transfer, trapping, and antenna size in
photosystem II. Biochemistry. 2001 Apr 3; 40(13): 4026-34.
- Kruse O, Hankamer B, Konczak C, Gerle C, Morris E, Radunz A, Schmid GH, Barber J.
Phosphatidylglycerol is involved in the dimerization of photosystem II. J Biol Chem. 2000 Mar 3; 275(9): 6509-14.
- Hankamer B, Morris EP, Barber J. Revealing the structure of the oxygen-evolving core dimer of photosystem II by
cryoelectron crystallography. Nat Struct Biol. 1999 Jun; 6(6): 560-4.
- Barber J, Nield J, Morris EP, Hankamer B. Subunit positioning in photosystem II revisited. Trends Biochem Sci. 1999 Feb; 24(2): 43-5. Review.
- Boekema EJ, Nield J, Hankamer B, Barber J. Localization of the 23-kDa subunit of the oxygen-evolving complex of photosystem II by electron microscopy. Eur J Biochem. 1998 Mar 1; 252(2): 268-76.
- Morris EP, Hankamer B, Zheleva D, Friso G, Barber J. The three-dimensional structure of a photosystem II core complex determined by electron crystallography.
Structure. 1997 Jun 15; 5(6): 837-49.
- Hankamer B, Nield J, Zheleva D, Boekema E, Jansson S, Barber J. Isolation and biochemical characterisation of monomeric and dimeric photosystem
II complexes from spinach and their relevance to the organisation of photosystem II in vivo. Eur J Biochem. 1997 Jan 15; 243(1-2): 422-9.
- Zheleva D, Hankamer B, Barber J. Heterogeneity and pigment composition of isolated photosystem II reaction centers. Biochemistry. 1996 Nov 26; 35(47): 15074-9.
- Boekema EJ, Hankamer B, Bald D, Kruip J, Nield J, Boonstra AF, Barber J, Rogner M. Supramolecular structure of the photosystem II complex from green plants and cyanobacteria. Proc Natl Acad Sci U S A. 1995 Jan 3; 92(1): 175-9.