Comparisons of NMR Spectral Quality and Success in Crystallization Demonstrate that NMR and X-ray Crystallography Are Complementary Methods for Small Protein Structure Determination
| Autor: | Rong Xiao, Thomas Acton, Jinfeng Liu, Philip C. Manor, M. Ciano, B. Rost, Gaetano T. Montelione, Paolo Rossi, Yang Chen, G.V.T. Swapna, P. A. Rajan, John P. Hunt, James M. Aramini, Natalia G. Denissova, David A. Snyder, Richard Karlin |
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| Rok vydání: | 2005 |
| Předmět: |
Proteomics
Magnetic Resonance Spectroscopy Crystallography X-Ray Biochemistry Protein Structure Secondary Catalysis law.invention Colloid and Surface Chemistry Protein structure Bacterial Proteins law Animals Humans Molecule Crystallization Chemistry Proteins General Chemistry Nuclear magnetic resonance spectroscopy NMR spectra database Crystallography Eukaryotic Cells Research Design X-ray crystallography Heteronuclear single quantum coherence spectroscopy |
| Zdroj: | Journal of the American Chemical Society. 127:16505-16511 |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | X-ray crystallography and NMR spectroscopy provide the only sources of experimental data from which protein structures can be analyzed at high or even atomic resolution. The degree to which these methods complement each other as sources of structural knowledge is a matter of debate; it is often proposed that small proteins yielding high quality, readily analyzed NMR spectra are a subset of those that readily yield strongly diffracting crystals. We have examined the correlation between NMR spectral quality and 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 demonstrates that, across this protein sample set, the quality of a protein's ( 15 N- 1 H)-heteronuclear correlation (HSQC) spectrum recorded under conditions generally suitable for 3D structure determination by NMR, a key predictor of the ability to determine a structure by NMR, is not correlated with successful crystallization and structure determination by X-ray crystallography. These results, together with similar results of an independent study presented in the accompanying paper (Yee, et al., J. Am. Chem. Soc., accompanying paper), demonstrate that X-ray crystallography and NMR often provide complementary sources of structural data and that both methods are required in order to optimize success for as many targets as possible in large-scale structural proteomics efforts. |
| Databáze: | OpenAIRE |
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