What’s the Fate of Structural Biology?

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In 1912, the German physicist Max Von Laue published the first paper demonstrating x-ray diffraction from a crystal.

In 1913, William Lawrence Bragg and William Henry Bragg(father and son) determined crystal structure of diamond.

In 1952, Rosalind Franklin used x-ray diffraction to image DNA and suggested it has a helical structure.

In 1958, John Kendrew and Max Perutz determined first protein structures of myoglobin and hemoglobin.

Thousands of structural biologists have worked for a century to solve molecular structures. To date, the Cambridge Structural Database have collected more than 600,000 structures of organic and organometallic molecules and the Protein Data Bank also contained about 100,000 Biological Macromolecular Structures. Based on the data in Protein Data Bank, ~88.5% of Biological Macromolecular Structures were solved by X-ray Crystallography, ~10.5% were solved by NMR and only ~1% were determined by Electron Microscopy. Obviously, structural biology, especially crystallography has made great achievements. UNESCO has declared 2014 to be the International Year of Crystallography

While recently,  The United States is winding down a $1 billion project to churn out protein structures. You can click on the following links to read details:

Structural Biology Scales Down

http://www.sciencemag.org/content/343/6175/1072.summary

Large NIH projects cut

http://www.nature.com/news/large-nih-projects-cut-1.14147

Crystallography at 100

http://www.sciencemag.org/site/special/crystallography/index.xhtml

http://www.nature.com/news/specials/crystallography-1.14540

What can structural biology bring us? What’s the fate of structural biology?

As we know, Structure Based Drug Design and High Throughput Screening are the two popular strategies in drug discovery and combining these two strategies should be a better choice. Therefore, excellent 3D structures would well advance drug discovery. What’s more, 3D structures of Biological Macromolecular can help us understand many biological phenomena in the atomic level. While, we have to say, using the same method, like crystallography, to determine plenty of structures rather than developing new or perfecting methodologies to overcome the weakness of current structure models. Try to imagine, what would happen if we could capture or even observe the native conformations and entire motion profile of biological macromoleculars. Will the tumor and other devastating diseases still be so terrible?

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