|Journal of the American Chemical Society (2005) 127(47):16505-11|
|Northeast Structural Genomics Consortium|
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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 [15N-1H]-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.
|Crystallography, X-Ray Humans Magnetic Resonance Spectroscopy Research Design Eukaryotic Cells Animals Proteomics Protein Structure, Secondary Proteins Bacterial Proteins |
|49 (Last update: 03/25/2017 11:30:18am)|
HTP NMR MicroCryoProbe Screening of Protein Samples
HTP NMR MicroCryoProbe screening of protein samples
|J Am Chem Soc. 2005 Nov 30;127(47):16505-11.|