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Protein Structure Preservation

The Protein Structure Initiative will wrap up next year, when its funding dries up, so plans should be made in advance about what will be done with the "valuable resources and expertise" it has generated, Allison Doerr writes in Nature.

The National Institute of General Medical Sciences launched the PSI at a time when determining protein structures was "painfully slow," and when NIH was flush with the kind of cash it needed to embark on the kind of long and grinding scientific voyages of discovery that PSI turned out to be.

But that was 15 years and about a billion dollars ago, and through its first two terms the PSI was drawing the ire of members of the structural biology community who said it focused too much on small bacterial protein structures that were not very interesting because they were low-hanging fruit. Now, in its third period, PSI-Biology, the program has targeted difficult structures like human membrane proteins and drug targets, which has "led to several successful structures for highly interesting yet difficult proteins such as GPCRs," Doerr writes.

The loss of the program will "shake up structural biology in the US," she says, and even will impact other researchers who benefit from PSI resources.

But now that PSI is in its waning period, NIGMS has an opportunity to wind this program down the right way, and minimize its impact. The institute has created internal and external planning committees to determine which PSI resources and capabilities should be preserved and how it should be done. NIGMS also is expected to announce this year what will happen to the substantial high-thorughput expression, purification, and crystallization facilities the program generated, Doerr says.

She says this infrastructure, and the large=scale raw data and metadata PSI generated should be preserved as much as possible, and that a smaller scale project to systematically sample protein folds should be continued on a much smaller scale. NIGMS also should continue to facilitate team research that looks into some particularly challenging structural biology research problems, she advises.

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