Recently installed infrastructure for automated protein nano-crystallisation, at Monash University, has important implications for the field of structural biology in Australia and internationally.

The platform, housed at Monash University, will be the first high-throughput robotic nano-crystallisation and imaging facility in Australia, paving the way for pioneering and world-class research in the field of molecular imaging.

Set to open its doors in July, the facility will also be equipped with the SONICC system (Second Order Nonlinear Imaging of Chiral Crystals), which is able to find crystals other technologies cannot.

SONICC technology relies on UV light and two photon excited fluorescence (UV-TPEF). Crystals appear white against a stark black background, helping users identify crystals even in cloudy conditions. This technology can distinguish between salt and protein crystals; detect sub-micron crystals (resulting in pictures that look like stars in the sky) and; facilitate detection of crystals in lipid cubic phase (LCP).

Crystallographers rely on crystal detection to carry out their experiment, either optimisation or structure determination. The SONICC will allow detection of virtually any crystal form such as microcrystals (<1µm), hiding behind precipitate, very fine plates or even crystals placed on the edge of the drop.

Crystals cannot hide anymore!!

The facility will feed into powerful imaging platforms, including the US and European XFELs, the Monash Micro-Electron Diffraction capable Titan KRIOS and the Australian Synchrotron.

Through building on existing expertise and advancing current facilities, the Monash Macromolecular Crystallisation Facility will enable researchers from academia and industry to study molecular structure through analysis of sub-micron sized crystals.

It will facilitate multidisciplinary collaboration across the spectrum of physics, immunology and biochemistry, which will open up new possibilities for solving complex macromolecular structures – such as 3D structures of integral membrane proteins.

The establishment of such a facility will help ensure that Australian research in structural biology remains top notch. Moreover, its very existence will help researchers overcome significant roadblocks: namely, the difficulties associated with crystallising challenging structural biology targets and reliably imaging protein nano-crystals.

Located at Monash University, the brand-new robotics will be managed by the protein crystallography platform. Its close proximity to the Australian Synchrotron and the Monash Ramaciotti Centre for Cryo-Electron Microscopy Monash will further enable development of diffraction techniques associated with the study of nano-crystals.

The facility will be accessible to all Australian researchers and it will support major ARC-funded research programmes, including that of the Imaging CoE. At Monash itself, the platform will further directly benefit more than 200 researchers and 25 major research groups.