Comparisons of NMR Spectral Quality and Success in Crystallization Demonstrate that NMR and X-ray Crystallography Are Complementary Methods for Small Protein Structure Determination

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• 作者：David A. Snyder ; Yang Chen ; Natalia G. Denissova ; Thomas Acton ; James M. Aramini ; Melissa Ciano ; Richard Karlin ; Jinfeng Liu ; Philip Manor ; P. A. Rajan ; Paolo Rossi ; G. V. T. Swapna ; Rong Xiao ; Burkha
• 刊名：Journal of the American Chemical Society
• 出版年：2005
• 出版时间：November 30, 2005
• 年：2005
• 卷：127
• 期：47
• 页码：16505 - 16511
• 全文大小：267K
• 年卷期：v.127,no.47(November 30, 2005)
• ISSN：1520-5126

文摘

X-ray crystallography and NMR spectroscopy provide the only sources of experimental datafrom which protein structures can be analyzed at high or even atomic resolution. The degree to whichthese methods complement each other as sources of structural knowledge is a matter of debate; it is oftenproposed that small proteins yielding high quality, readily analyzed NMR spectra are a subset of those thatreadily yield strongly diffracting crystals. We have examined the correlation between NMR spectral qualityand success in structure determination by X-ray crystallography for 159 prokaryotic and eukaryotic proteins,prescreened to avoid proteins providing polydisperse and/or aggregated samples. This study demonstratesthat, across this protein sample set, the quality of a protein's [¹⁵N-¹H]-heteronuclear correlation (HSQC)spectrum recorded under conditions generally suitable for 3D structure determination by NMR, a key predictorof the ability to determine a structure by NMR, is not correlated with successful crystallization and structuredetermination by X-ray crystallography. These results, together with similar results of an independent studypresented in the accompanying paper (Yee, et al., J. Am. Chem. Soc., accompanying paper), demonstratethat X-ray crystallography and NMR often provide complementary sources of structural data and that bothmethods are required in order to optimize success for as many targets as possible in large-scale structuralproteomics efforts.