The TOPAZ® system for protein crystallization has figured prominently in structure-based research on receptor specificity of the hemagglutinin (HA) from an H5N1 avian influenza virus, commonly known as "avian flu".
The goal of this research was to identify mutations that can permit influenza A viruses to cross the species barrier and adapt to a new host.
The TOPAZ system allowed researchers to efficiently identify initial leads for solving the HA structure.
Continued outbreaks of the H5N1 virus in poultry and wild birds make the potential emergence of a human-adapted H5 virus a growing threat.
"We are thrilled that TOPAZ played a role in this discovery, and, given the importance of the project, that results were obtained so quickly," said Gajus Worthington, CEO of Fluidigm.
The study was published in the April 21st 2006 issue of Science Magazine. The work represents a collaboration of investigators from several US public research organizations.
"We used the TOPAZ system to conduct initial crystallization trials, which allowed us to rapidly identify suitable crystallization conditions while conserving our valuable baculovirus expressed H5 hemagglutinin for other project needs," said Ian Wilson, Professor at The Scripps Research Institute.
"Translation of the conditions into sitting drops was focused on the most promising initial hits, again helping to conserve precious resources. These crystals were then used for X-ray structure determination."
The TOPAZ X.96 screening chips are capable of running up to 768 experiments in parallel with as little as 10 nanoliters of protein per condition.
To match pace with this experimental throughput, Dr. Wilson's group uses the TOPAZ AutoInspeX® workstation, which streamlines the process of downstream analysis by automating the scoring of crystallization results.
This latest structure discovery from The Scripps Research Institute is one of several linked to customers of the TOPAZ system that are expected for publication this year.