New method opens crystal clear views of biomolecules

[n2doc]

A scientific breakthrough gives researchers access to the blueprint of thousands of molecules of great relevance to medicine and biology. The novel technique, pioneered by a team led by DESY scientist Professor Henry Chapman from the Center for Free-Electron Laser Science CFEL and reported this week in the scientific journal Nature, opens up an easy way to determine the spatial structures of proteins and other molecules, many of which are practically inaccessible by existing methods. The structures of biomolecules reveal their modes of action and give insights into the workings of the machinery of life. Obtaining the molecular structure of particular proteins, for example, can provide the basis for the development of tailor-made drugs against many diseases. "Our discovery will allow us to directly view large protein complexes in atomic detail," says Chapman, who is also a professor at the University of Hamburg and a member of the Hamburg Centre for Ultrafast Imaging CUI.

To determine the spatial structure of a biomolecule, scientists mainly rely on a technique called crystallography. The new work offers a direct route to "read" the atomic structure of complex biomolecules by crystallography without the usual need for prior knowledge and chemical insight. "This discovery has the potential to become a true revolution for the crystallography of complex matter," says the chairman of DESY's board of directors, Professor Helmut Dosch.

In crystallography, the structure of a crystal and of its constituents can be investigated by shining X-rays on it. The X-rays scatter from the crystal in many different directions, producing an intricate and characteristic pattern of numerous bright spots, called Bragg peaks (named after the British crystallography pioneers William Henry and William Lawrence Bragg). The positions and strengths of these spots contain information about the structure of the crystal and of its constituents. Using this approach, researchers have already determined the atomic structures of tens of thousands of proteins and other biomolecules.

But the method suffers from two significant barriers, which make structure determination extremely difficult or sometimes impossible. The first is that the molecules must be formed into very high quality crystals. Most biomolecules do not naturally form crystals. However, without the necessary perfect, regular arrangement of the molecules in the crystal, only a limited number of Bragg peaks are visible. This means the structure cannot be determined, or at best only a fuzzy "low resolution" facsimile of the molecule can be found. This barrier is most severe for large protein complexes such as membrane proteins. These systems participate in a range of biological processes and many are the targets of today's drugs. Great skill and quite some luck are needed to obtain high-quality crystals of them.

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http://www.sciencedaily.com/releases/2016/02/160210134653.htm

If this ends up being widely applicable, it is a very big deal.

[Wounded Bear]

1. Sounds promising and very useful...

thanks for the link.

[eppur_se_muova]

2. Now *that* was a well and clearly written article.

I have enough background in intro. XRD to know what they're talking about, just not the full-blown mathematics of it.

[gregcrawford]

3. Ah loves me summa that scientifical stuff!

Just kidding! We who are uninitiated might like to know a little more about the processes involved in crystalizing biological molecules.

Making such arcane information accessible to laypersons like myself is testament to the skill of the writer. After reading the article, my first thought was to compare these early stages of the discovery to a dot matrix printer of yesteryear, and their goal to the finest photo printers of today. I can see this having a monumental impact in the not too distant future.