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Macromolecular crystallography and what it can contribute to antiparasite drug discovery

[Acta F logo]
[Bo1A structure] Solution-state NMR structure of BolA (PFE0790c) from P. falciparum [Buchko, G. W. et al. (2015). Acta Cryst. F71, 514-521].

The May 2015 issue of Acta Crystallographica Section F Structural Biology Communications ( is a dedicated special issue on the structural investigation of proteins associated with molecular parasitology, specifically research linked to protozoan pathogens. Parasitic protozoa threaten the lives of millions of human beings by causing a range of diseases including malaria, leishmaniasis, Chagas disease, toxoplasmosis and African sleeping sickness.

[Orotate complex] P. falciparum dihydro-orotate dehydrogenase complex with DSM267 and FMN [Hol, W. G. J. (2015). Acta Cryst. F71, 485-499].

Researchers have sought to understand the processes that allow pathogens to exist, to invade a host, to evade the immune response and to cause these debilitating and often fatal diseases. Structural biology, and in particular crystallography, complements such investigations. It can play a key role in drug discovery by providing accurate chemical information to guide the assessment of drug targets and computational design projects, in the search for pharmaceutical compounds.

This special issue includes fundamental studies in molecular parasitology and also research directed toward protozoan drug target characterization, including both NMR and crystal structures. The articles include an overview and perspective from Wim Hol, an inspirational champion for the role of crystallography in drug discovery. There is also a short review from Inari Kursula on cytoskeletal proteins related to the infection process, a topic that may provide opportunities in future drug discovery work.

The publication of this special issue represents an exciting new departure for Acta Crystallographica Section F. The journal hopes to provide a natural home for new research in molecular parasitology, as well as welcoming contributions from the structural biology community as a whole.