English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment.

MPS-Authors
/persons/resource/persons15732

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

/persons/resource/persons14824

Becker,  S.
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
No external resources are shared
Fulltext (public)

332899.pdf
(Publisher version), 0B

Supplementary Material (public)
There is no public supplementary material available
Citation

Rumpel, S., Becker, S., & Zweckstetter, M. (2008). High-resolution structure determination of the CylR2 homodimer using paramagnetic relaxation enhancement and structure-based prediction of molecular alignment. Journal of Biomolecular NMR, 40(1), 1-13. Retrieved from http://springerlink.metapress.com/content/15r81702p04t73p2/fulltext.pdf.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-DD4F-E
Abstract
There is no abstract available