During the drug design process, to probe about and know the structure of proteins is of great importance to grasp the specific medical potential and performance, as well as their safety profiles. Crystallization and X-ray crystallography are commonly involved in such inspecting and testing. But they are preferred by big crystals that are hard to be formed for complex proteins and are incline to be influenced by the radiation beam.
A new tech x-ray serial crystallography is innovative in this aspect in recent years to increase the capturing times of the protein structure. However, a big issue was encountered to achieve the best result with this new tech. When transfer the crystals from their growing chips, there is lose caused by the damages in their structure. And to grow the crystals right on the chip where they will be x-rayed is limited by the thickness of the device, which will bring new problems like limited signal to noise ratio, sample evaporation and so on.
To better address this problem, research team from the University of Massachusetts Amherst led by Sarah Perry found a solution that can assist the tech to achieve its most potential by adding a graphene layer into the crystallography device.
The outstanding characters of the upgraded device lie in its strong ability to preserve the hydration state of the crystals that are significant in protecting the molecular integrity and its high transferring ratio from signal to noise. “
In the experiments with hen egg white lysosome, the team collected a great signal-to-noise level with X-ray diffraction measurements in the optimized device. Being highly thought of by the professionals in this field for its simple adjustment but great advance in performance, the new tech will be widely applied for more flexible researches.
It’s reported that the team is now working to make the device smaller in size and more comprehensive in protein structure analysis while accessible to more various proteins.
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