1xn8

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Revision as of 07:04, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1xn8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xn8" /> '''Solution Structure of Bacillus subtilis Prot...)
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1xn8

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Solution Structure of Bacillus subtilis Protein yqbG: The Northeast Structural Genomics Consortium Target SR215

OverviewOverview

A standardized protocol enabling rapid NMR data collection for, high-quality protein structure determination is presented that allows one, to capitalize on high spectrometer sensitivity: a set of five G-matrix, Fourier transform NMR experiments for resonance assignment based on highly, resolved 4D and 5D spectral information is acquired in conjunction with a, single simultaneous 3D 15N,13C(aliphatic),13C(aromatic)-resolved, [1H,1H]-NOESY spectrum providing 1H-1H upper distance limit constraints., The protocol was integrated with methodology for semiautomated data, analysis and used to solve eight NMR protein structures of the Northeast, Structural Genomics Consortium pipeline. The molecular masses of the, hypothetical target proteins ranged from 9 to 20 kDa with an average of, approximately 14 kDa. Between 1 and 9 days of instrument time were, invested per structure, which is less than approximately 10-25% of the, measurement time routinely required to date with conventional approaches., The protocol presented here effectively removes data collection as a, bottleneck for high-throughput solution structure determination of, proteins up to at least approximately 20 kDa, while concurrently providing, spectra that are highly amenable to fast and robust analysis.

About this StructureAbout this Structure

1XN8 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

NMR data collection and analysis protocol for high-throughput protein structure determination., Liu G, Shen Y, Atreya HS, Parish D, Shao Y, Sukumaran DK, Xiao R, Yee A, Lemak A, Bhattacharya A, Acton TA, Arrowsmith CH, Montelione GT, Szyperski T, Proc Natl Acad Sci U S A. 2005 Jul 26;102(30):10487-92. Epub 2005 Jul 18. PMID:16027363

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