1. Research Expertise
  2. Collaborations
  3. Publications
Research Expertise -

Current Research Interests

I am currently involved in work on the following areas:

  • Development of applied methods using in-situ plate screening
  • Beamline automation and instrumentation
  • Structural biology (protein-ligand interactions)

In-situ plate screening

We are looking at developing applied methods in crystallography, by taking advantage of the high-throughput in-situ plate screening setup of the beamline (10 to 15 conditions can be screened per hour). As such, we have implemented a simple and relatively fast dehydration procedure that allows, in a single experiment, a comprehensive screening of the dehydration effect on protein crystals with X-ray feedback. In collaboration with Petra Lukacik, we have applied this method to a membrane-associated protein and monitored the effect of the dehydration on the crystals by following the shrinkage of the cell parameters. In this case, the result of dehydration also led to an improvement of the crystal’s diffraction from 2.9 Å resolution to 2.45 Å. We are further evaluating this method for membrane protein crystals in collaboration with Isabel De Moraes from the Membrane Protein Laboratory (MPL).

I would welcome enquiries from interested users for further information on this method, as well as potential collaborations.

Beamline automation

In collaboration with Irelec and I24 beamline, we have developed an end-effector compatible with the CATS robot (Irelec) and the unipuck sample holder (16 samples per puck) for a high capacity and faster sample exchange system. The prototype is currently running at the beamline with an exchange time reduced from 150 seconds to 37 seconds. We are also looking into easing the transition from the cryogenic experiments using the robot in the cryotong mode to the plate screening mode at room temperature. This improvement would enhance the flexibility of the beamline allowing users to operate two modes within their allocated 24-hours beamtime.  

Protein-ligand interactions

My previous experience in the pharmaceutical industry involved work on the characterisation of protein-small molecule complexes for the design of drug molecules using primarily protein crystallography but also other biophysical methods. X-ray crystallography is a very powerful tool in drug discovery, enabling a rational design based on the knowledge of the atomic details of protein-ligand interactions. Methionine aminopeptidase (MetAP) is a metalloprotease that removes the N-terminal methionine during protein synthesis and is essential for bacterial survival. Mycobacterium tuberculosis expresses two methionine aminopeptidases, MtMetAP1a and MtMetAP1c and both are potential targets to develop novel antitubercular therapeutics. There is accumulating biochemical evidence that both forms have large differences in their active site and therefore could potentially lead to different classes of inhibitors.  Several constructs of both MtMetAP1a and MtMetAP1c are currently being investigated as part of the protein 100 project at the Oxford Protein Production Factory (OPPF), to understand the selectivity of both forms, and might be the foundation for structure-based small molecule design projects.

Collaborations - +


Isabel De Moraes (Membrane Protein Laboratory @ Diamond Light Source, UK)

Matthieu Privat De Fortuné and Kenji Laroche (Irelec, Grenoble, France)

Ray Owen, Louise Bird, Jo Nettleship, Yamini Reddivari (Oxford Protein Production Factory, Research complex @ Harwell science and innovation campus, UK)

Jose Brandao-Neto, Pierre Aller, Petra Lukacik  (Diamond Light Source, UK)

Publications - +



A. Douangamath, P. Aller, P. Lukacik, J. Sanchez-Weatherby, I. De Moraes, J. Brandao-Neto (manuscript in preparation). Using high-throughput in-situ plate screening to evaluate the effect of dehydration on protein crystals.
J. Brandao-Neto, A. Douangamath, R. Fearn, J. Aishima, J. O’Hea, G. Preece, J. Williams, A. Marshall (manuscript in preparation). I04-1, a fixed wavelength, high-throughput and versatile MX beamline at Diamond Light Source.
A. Douangamath, J. Brandao-Neto, R. Flaig, J. Aishima, R. Fearn, G. Winter and A. Ashton. (2011). I04-1, a fixed-wavelength protein crystallography station in its first year of operations,  Acta Cryst. A67, C278.
A. Mac Sweeney, R. Lange, R.P. Fernandes, H. Schulz, G. E. Dale, A. Douangamath, P.J. Proteau, C. Oefner (2005). The crystal structure of E.coli 1-deoxy-D-xylulose-5-phosphate reductoisomerase in a ternary complex with the antimalarial compound fosmidomycin and NADPH reveals a tight-binding closed enzyme conformation. J Mol Biol. 345(1):115-27
A. Douangamath, G. E. Dale, A. D'Arcy, M. Almstetter, R. Eckl, A. Frutos-Hoener, B. Henkel, K. Illgen, S. Nerdinger, H. Schulz, A. Mac Sweeney, M. Thormann, A. Treml, S. Pierau, S. Wadman, C. Oefner (2004). Crystal structures of Staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate. J Med Chem. 47(6):1325-8.
C. Oefner, A. Douangamath, A. D'Arcy, S. Häfeli, D. Mareque, A. Mac Sweeney, J. Padilla, S. Pierau, H. Schulz, M. Thormann, S. Wadman, G. E. Dale (2003). The 1.15A crystal structure of the Staphylococcus aureus methionyl-aminopeptidase and complexes with triazole based inhibitors. J Mol Biol. 332(1):13-21.
A. Douangamath, F. V. Filipp, A. T. Klein, P. Barnett, P. Zou, T. Voorn-Brouwer, M. C. Vega, O. M. Mayans, M. Sattler, B. Distel, M. Wilmanns (2002). Topography for independent binding of alpha-helical and PPII-helical ligands to a peroxisomal SH3 domain. Mol Cell. 10(5):1007-17.
A. Douangamath, M. Walker, S. Beismann-Driemeyer, M. C. Vega-Fernandez, R. Sterner, M. Wilmanns (2002) Structural evidence for ammonia tunneling across the (beta alpha)(8) barrel of the imidazole glycerol phosphate synthase bienzyme complex. Structure. 10(2):185-93.
B. Fazi, M. J. Cope, A. Douangamath, S. Ferracuti, K. Schirwitz, A. Zucconi, D. G. Drubin, M. Wilmanns, G. Cesareni, L. Castagnoli (2002) Unusual binding properties of the SH3 domain of the yeast actin-binding protein Abp1: structural and functional analysis. J Biol Chem. 277(7):5290-8.
M. C. Vaney, I. Broutin, P. Retailleau, A. Douangamath, S. Lafont, C. Hamiaux, T. Prangé, A. Ducruix, M. Riès-Kautt (2001). Structural effects of monovalent anions on polymorphic lysozyme crystals. Acta Crystallogr D Biol Crystallogr. 57(Pt 7):929-40.

Alice Douangamath


Alice is a Senior Support Scientist for I04-1. She studied Physics at the University Paris 7 (France) and completed a joint PhD (University Orsay, France and EMBL-Hamburg, Germany) in biophysical characterisation of protein interactions. Alice then moved to the pharmaceutical industry (Morphochem, Switzerland and Evotec Ltd, UK) where, as a crystallographer, she was involved in structure-based drug design projects, before joining Diamond in 2007.

Email: alice.douangamath@diamond.ac.uk
Tel: +44 (0) 1235 778922

Key Research Area

Key Research Area

In-situ plate screening methods development, beamline automation, protein-ligand/small molecule interactions

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