Our body consists of countless molecules: water, micro- and macro-elements, sugars, fatty acids, proteins and others.

We function as precise, self-regulated machines, in which every single part has it's own role. 

Proteins, tiny structures with fully determined behaviour by the 3D structure, are designed to fulfill very specific tasks.

To control a process they have to collaborate with each other: some need to form complicated aggregates, others attach to a non-protein molecule, which allows for changing their 3D arrangement and function afterwards.

Some perform their tasks swimming freely around while others are bound into liquid-crystal structures called membranes.

The direct dependency between protein structure and function makes it very important to uncover atomic, 3D construction of these micro machines.

This would be an only way, that scientists are able to assess and verify proteins' exact role in both physiological and pathological processes.

The technique that allows for this examination is called X-ray crystallography.

In traditional X-ray crystallography, scientists have to obtain crystals of the protein under study and then manually transfer them, one by one, to the measuring device.

Relocated crystals are cooled down by liquid nitrogen and subjected to X-ray examination.

Although the freezing reduces crystal damage, it pushes it away from the natural confirmation and sometimes makes it crack thereby ruining the whole process.

A new pioneering method developed by biochemists from Trinity College, Dublin addresses most of the bottlenecks of traditional crystallization.

The in meso in situ serial crystallography (IMISX) excludes the burdensome crystal transfers, providing instead a intriguing possibility to study their structure in situ - meaning in the place in which they grew.

Small crystals grow in cyclic olefin copolymer (COC), a material mimicking natural cell membrane.

COC is cheap, easily accessible and works well under X-ray examination.

No cooling before the measurements is required, which means that the crystals are as close to their native structure as possible.

In addition, COC plates are resistant and easy to transport. 

IMISX method is promising in that, crystallography could become automated in the future.

Multiple crystals grown on the same plates could be measured sequentially if specific hardware and software techniques are developed.

This could make the whole process even more efficient and results oriented.

Professor Zongchao Jia, biochemist and crystallography expert (Queen's University, Ontario, Canada), who is not directly related to the study says, "This new paper represents yet another step in the right direction of promoting wider acceptance by the protein crystallography community. The improved apparatus would facilitate in meso experiment."

Why is this such a breakthrough discovery?

Crystallography lays the foundation for research that aims to improve life quality and expectation.

This includes not only understanding the mechanisms of diseases, but also developing new therapies and targeting unwanted molecules.

Advancements in the fields of vaccine and drug development rely greatly on the knowledge obtained by protein crystallography. 

By making the complex, error prone crystallographic procedure more reliable and automated, IMISX method encourages further advancements towards efficient protein X-ray crystallization.

"There are still many challenges associated with this method and further improvement in terms of ease of use and affordability is needed" added Professor Jia.

It will certainly change the pace of protein structure discoveries and hopefully boost the capacity of the pharmaceutical industry as well.

 

 

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