Argonne National Laboratory in Illinois reports that researchers have come a step closer to a cure for the most common strain of avian flu, the potential pandemic that has claimed more than 200 lives and infected nearly 400 people in 14 countries since it was identified in 2003.

The research was funded by a number of agencies in China and the USA and carried out by scientists at the US Department of Energy's Argonne National Laboratory, in conjunction with researchers in China and Singapore.

Together, they have crystallised and characterised the structure of one of the most important protein complexes of the H5N1 virus, the most common strain of avian flu.

All viruses, including H5N1, contain only a small number of proteins that govern all of the virus functions. In H5N1, one of the most important of these proteins is RNA polymerase. Comprising three sub-units - PA, PB1 and PB2 - it contains all the instructions that allow the virus to copy itself.

Following X-ray crystallography of the protein crystals, Argonne biophysicist Andrzej Joachimiak explained, "When we mapped out the PA sub-unit, it looked very much like the head of a dragon. One domain looked like the dragon's brains, and the other looked like its mouth."

During RNA replication, the three sub-units of the protein come together, and the scientists noticed that one end of the PB1 sub-unit must bind to the 'dragon's mouth' of the PA sub-unit.

It is hoped that muzzling the 'dragon's mouth' could be used to develop of therapies and/or vaccines against H5N1.

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