Full details of this facility and its available services can be found at http://uqrocx.imb.uq.edu.au.


The UQ Remote Operation Crystallisation and X-ray Diffraction (UQ ROCX) Facility provides research training and support for protein structure determination.

This support includes protein crystallisation condition screening, crystal diffraction screening, data collection, data processing, and structure determination. Nano-litre liquid handlers and automated imaging means that large numbers of crystallisation conditions can be investigated with small quantities of protein. The diffraction facility has Queensland’s brightest research X-ray source and the state’s only robotic sample storage and retrieval system, which allows for multiple data sets to be collected without user intervention.

In 2013, 61 unique users accessed the facility for its high-throughput applications, namely crystallisation condition screening, especially for membrane proteins; and screening fragment libraries for drug leads.

Collectively, users performed 100,000 crystallisation experiments, collected 56 diffraction data sets and published 15 scientific papers supported by UQ ROCX access in 2013.

Some of the discoveries reported in 2013 using the facility included identification and characterisation of a protein essential for pathogenicity in the infectious disease melioidosis, and a potential bioweapon; characterisation of the mechanism by which cells use PX-FERM proteins to move diverse transmembrane cargos around the body; the discovery and characterisation of potent enzyme inhibitors with antimalarial activity; and the discovery of how bacteria find the specific metals they need to function.

UQ ROCX is funded by the Australian Research Council and UQ.


Facility contacts

Facility Manager and Radiation Safety Officer: Karl Byriel
E-mail: k.byriel@uq.edu.au

Crystallisation Officer: Dr Gordon King
E-mail: g.king@uq.edu.au

Director, UQROCX: Professor Jennifer Martin
E-mail: j.martin@uq.edu.au

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