1XNE

Solution Structure of Pyrococcus furiosus Protein PF0470: The Northeast Structural Genomics Consortium Target PfR14

Summary for 1XNE

• Entry DOI: 10.2210/pdb1xne/pdb
• Descriptor: hypothetical protein PF0469 (1 entity in total)
• Functional Keywords: gft nmr, structural genomics, protein structure initiative, psi, nesg, pfr14, alpha and beta protein, northeast structural genomics consortium, unknown function
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 13817.35

Authors

Liu, G.,Xiao, R.,Parish, D.,Ma, L.,Sukumaran, D.,Acton, T.,Montelione, G.T.,Szyperski, T.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2004-10-04, release date: 2004-12-14, Last modification date: 2024-05-01)

Primary citation

Liu, G.,Shen, Y.,Atreya, H.S.,Parish, D.,Shao, Y.,Sukumaran, D.K.,Xiao, R.,Yee, A.,Lemak, A.,Bhattacharya, A.,Acton, T.A.,Arrowsmith, C.H.,Montelione, G.T.,Szyperski, T.
NMR data collection and analysis protocol for high-throughput protein structure determination.
Proc.Natl.Acad.Sci.Usa, 102:10487-10492, 2005

PubMed Abstract: 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.

PubMed: 16027363
DOI: 10.1073/pnas.0504338102

Experimental method

SOLUTION NMR