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

NMR in the SPINE Structural Proteomics project

Ab, E., Atkinson, A., Banci, L., Bertini, I., Ciofi-Baffoni, S., Brunner, Konrad, Diercks, T. , Dötsch, V., Engelke, F., Folkers, G., Griesinger, C., Gronwald, W., Günther, U., Habeck, M. , Jong, R. , Kalbitzer, Hans-Robert, Kieffer, B. , Leeflang, B. , Loss, S., Luchinat, C. , Marquardsen, T., Moskau, D., Neidig, K., Nilges, M. , Piccioli, M. , Pierattelli, R. , Rieping, W., Schippmann, T., Schwalbe, H. , Travé, G., Trenner, Jochen, Wöhnert, J., Zweckstetter, M. and Kaptein, R. (2006) NMR in the SPINE Structural Proteomics project. Acta Crystallographica Section D D 62 (10), pp. 1150-1161.

Date of publication of this fulltext: 05 Aug 2009 13:34
Article
DOI to cite this document: 10.5283/epub.1887


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 ...

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 protonless C-13-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.



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Details

Item typeArticle
Journal or Publication TitleActa Crystallographica Section D
Publisher:BLACKWELL PUBLISHING
Place of Publication:OXFORD
Volume:D 62
Number of Issue or Book Chapter:10
Page Range:pp. 1150-1161
Date2006
InstitutionsBiology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie
Identification Number
ValueType
10.1107/S0907444906032070DOI
KeywordsPROTEIN-BACKBONE ASSIGNMENT; NUCLEOTIDE EXCISION-REPAIR; COPPER TRAFFICKING PROTEIN; AUTOMATED NOE ASSIGNMENT; HUMAN BETA-PARVALBUMIN; CYTOCHROME-C-OXIDASE; SOLID-STATE NMR; PARAMAGNETIC PROTEINS; EFFICIENT STRATEGY; ALPHA-PARVALBUMIN;
Dewey Decimal Classification500 Science > 570 Life sciences
StatusPublished
RefereedYes, this version has been refereed
Created at the University of RegensburgYes
Item ID1887

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