Solid state NMR sequential resonance assignments and conformational analysis of 
the 2 x 10.4 kDa dimeric form of the Bacillus subtilis protein Crh

Boeckmann, A.; Lange, A.; Galinier, A.; Luca, S.; Giraud, N.; Juy, M.; Heise, H.; Montserret, R.; Penin, F.; Baldus, M.

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Solid state NMR sequential resonance assignments and conformational analysis of the 2 x 10.4 kDa dimeric form of the Bacillus subtilis protein Crh

MPS-Authors

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Lange, A.
Research Group of Solid-State NMR, MPI for biophysical chemistry, Max Planck Society;

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

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Heise, H.
Research Group of Solid State NMR Spectroscopy, MPI for biophysical chemistry, Max Planck Society;

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Baldus, M.
Research Group of Solid State NMR Spectroscopy, MPI for biophysical chemistry, Max Planck Society;

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Boeckmann, A., Lange, A., Galinier, A., Luca, S., Giraud, N., Juy, M., et al. (2003). Solid state NMR sequential resonance assignments and conformational analysis of the 2 x 10.4 kDa dimeric form of the Bacillus subtilis protein Crh. Journal of Biomolecular NMR, 27(4), 323-339. Retrieved from http://springerlink.metapress.com/content/hm7nn33035w37551/fulltext.pdf.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-EF95-1

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