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NMR Hits the Big Time

When it comes to structural biology, bigger really is better. Most biological processes are performed by enormous multicomponent complexes, such as the ribosome. To solve the structures of these monsters, biologists traditionally have used two different but complementary techniques, nuclear magnetic resonance (NMR) and X-ray crystallography. They have had considerable success using the latter technique for protein structure determination, but the former technique has lagged behind, in part be

Aileen Constans

When it comes to structural biology, bigger really is better. Most biological processes are performed by enormous multicomponent complexes, such as the ribosome. To solve the structures of these monsters, biologists traditionally have used two different but complementary techniques, nuclear magnetic resonance (NMR) and X-ray crystallography. They have had considerable success using the latter technique for protein structure determination, but the former technique has lagged behind, in part because it has not been possible to apply NMR to proteins larger than about 30,000 daltons (Da).

But now NMR is catching up. New procedures and a procession of ever-larger magnets have helped researchers chip away at the size ceiling that has constrained them. The biggest of the big: ultrahigh-field 900-MHz instruments. These systems improve peak resolution, enabling spectroscopists to focus on ever-larger molecules. And because the instrument's sensitivity increases with the magnetic field strength, stronger magnets permit experiments to be run...

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