NMR in the SPINE Structural Proteomics project

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 62; no. 10; pp. 1150 - 1161
• Main Authors: 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.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England Blackwell Publishing Ltd 01-10-2006
• Subjects: Algorithms; Data Interpretation, Statistical; high throughput; interferential structure determinations; Magnetic Resonance Spectroscopy - methods; Models, Molecular; NMR spectroscopy; Proteins - chemistry; Proteomics - methods; protonless13C-direct detection methods
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444906032070

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.