NMR in the SPINE structural proteomics project.

Ab, E.; Atkinson, A. R.; Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Brunner, K.; Diercks, T.; Dötsch, V.; Engelke, F.; Folkers, G. E.; Griesinger, C.; Gronwald, W.; Günther, U.; Habeck, M.; De Jong, R. N.; Kalbitzer, H. R.; Kieffer, B.; Leeflang, B. R.; Loss, S.; Luchinat, C.; Marquardsen, T.; Moskau, D.; Neidig, K. P.; Nilges, M.; Piccioli, M.; Pierattelli, R.; Rieping, W.; Schippmann, T.; Schwalbe, H.; Travé, G.; Trenner, J.; Wöhnert, J.; Zweckstetter, M.; Kaptein, R.

doi:10.1107/S0907444906032070

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

NMR in the SPINE structural proteomics project.

MPS-Authors

/persons/resource/persons15147

Griesinger, C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter, M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

External Resource

http://onlinelibrary.wiley.com/doi/10.1107/S0907444906032070/pdf
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Ab, E., Atkinson, A. R., Banci, L., Bertini, I., Ciofi-Baffoni, S., Brunner, K., et al. (2006). NMR in the SPINE structural proteomics project. Acta Crystallographica Section D-Biological Crystallography, 62(10), 1150-1161. doi:10.1107/S0907444906032070.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000E-7096-2

Abstract

This paper describes the developments, role and contributions of the NMR spectroscopy groups in the Structural Proteomics In Europe (SPINE) consortium. Focusing on the development of high-throughput (HTP) pipelines for NMR structure determinations of proteins, all aspects from sample preparation, data acquisition, data processing, data analysis to structure determination have been improved with respect to sensitivity, automation, speed, robustness and validation. Specific highlights are protonless13C-direct detection methods and inferential structure determinations (ISD). In addition to technological improvements, these methods have been applied to deliver over 60 NMR structures of proteins, among which are five that failed to crystallize. The inclusion of NMR spectroscopy in structural proteomics pipelines improves the success rate for protein structure determinations.