Volume 92 Issue 5 | p. 6 | News of The Week
Issue Date: February 3, 2014 | Web Date: January 30, 2014

NMR Structures Get Sharper With Rosetta

Computer program refines nuclear magnetic resonance structures of proteins, making them more similar to X-ray crystal structures
Department: Science & Technology | Collection: Life Sciences
News Channels: Analytical SCENE, Biological SCENE, JACS In C&EN
Keywords: nuclear magnetic resonance spectroscopy, Rosetta, X-ray crystallography, protein structure, structural biology

For determining protein structure, X-ray crystallography typically beats nuclear magnetic resonance spectroscopy for accuracy. But chemists now report that, in most cases, NMR structures refined by a computer program called Rosetta match more closely with those determined by crystallography than do unrefined ones.

Although X-ray crystallography is the gold standard for solving protein structures, not all proteins crystallize well. Also, floating in solution could be a more realistic condition for proteins than sitting in a . . .

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