"Crystal Hotel" in Biochemistry Department.



Professor Kurt Krause and Dr Peter Mace with the crystal hotel.

The Department of Biochemistry has taken delivery of a new  ‘Rock Imager’ crystal growth and imaging facility.

The Rock Imager, from Formulatrix, the leading crystal imaging platform available, allows researchers to simultaneously keep 190 plates in a temperature controlled environment, and automatically capture images of every experiment on any fixed schedule. This capacity means users can track up to 50,000 individual crystallisation trials, and check their progress from anywhere in the world over the internet. The facility has been established through combined support from a University of Otago Large Equipment Grant, a grant from Lotteries Health Research, and additional contributions from the Department of Biochemistry, Department of Microbiology and Immunology, School of Pharmacy, and Faculty of Dentistry, as well as the Otago School of Medical Sciences and the Division of Health Sciences.

 Knowledge of the exact three-dimensional structure of proteins and their complexes underpins many areas of biology. The most widely used method for determining protein structures is X-ray crystallography, which has been successfully used for decades and is used by groups at Otago across the Division of Health Sciences. However, determining a structure still hinges on the ability to grow crystals of that protein. In a typical crystallization experiment researchers will test a protein against ~500 or more chemicals, then each experiment must be checked individually in a regular manner. Traditionally this has been performed by hand using a standard light microscope. Modern projects demand the observation of protein crystallization experiments on a scale that is difficult to achieve manually. Aside from the time and physical challenge of observing thousands of microscopic experiments, manual observation misses transient crystals and tends to falsely report positive crystals. This is not surprising, given that we are only human and each crystallisation experiment is a tiny drop about 2 mm across, and ‘good’ crystals that do grow are normally less than 0.1 mm. Protein crystals that do grow are then exposed to powerful X-ray beams that allow researchers to determine the exact three-dimensional arrangement of atoms in that protein.

“The beauty of automated imaging is we can catch crystals that grow then disappear, or tell when a crystal has stopped growing and is ready to be harvested”, says Dr. Peter Mace who, with Professor Kurt Krause, has overseen establishment of the facility. “After only a few weeks we have already caught crystals that we would have missed otherwise, and now have new leads to follow up”.

Read the full story on the university website.