Lining Up Proteins for NMR

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Science  07 Nov 1997:
Vol. 278, Issue 5340, pp. 1015-1016
DOI: 10.1126/science.278.5340.1015

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X-ray crystallography has a troublesome shortfall: It can pinpoint the location of atoms with extreme accuracy when proteins are stacked in a crystal, but many proteins don't readily form such regular assemblies. Nuclear magnetic resonance (NMR) spectroscopy, on the other hand, can map proteins in their native solution environment, but it has never been able to match the peak precision of its rival. Now on page 1111, two NMR experts report on a new technique that gently aligns the protein molecules in a bath of liquid crystals, allowing researchers to determine how each bond between neighboring atoms is oriented with respect to the rest of the molecule.