Paramagnetic shifts in solid-state NMR of proteins to elicit structural information

Stéphane Balayssac, Ivano Bertini, Anusarka Bhaumik, Moreno Lelli, Claudio Luchinat

Research output: Contribution to journalArticlepeer-review

75 Scopus citations


The recent observation of pseudocontact shifts (pcs) in 13C high-resolution solid-state NMR of paramagnetic proteins opens the way to their application as structural restraints. Here, by investigating a microcrystalline sample of cobalt(II)-substituted matrix metalloproteinase 12 [CoMMP-12 (159 AA, 17.5 kDa)], it is shown that a combined strategy of protein labeling and dilution of the paramagnetic species (i.e., 13C-,15N- labeled CoMMP-12 diluted in unlabeled ZnMMP-12, and 13C-, 15N-labeled ZnMMP-12 diluted in unlabeled CoMMP-12) allows one to easily separate the pcs contributions originated from the protein internal metal (intramolecular pcs) from those due to the metals in neighboring proteins in the crystal lattice (intermolecular pcs) and that both can be used for structural purposes. It is demonstrated that intramolecular pcs are significant structural restraints helpful in increasing both precision and accuracy of the structure, which is a need in solid-state structural biology nowadays. Furthermore, intermolecular pcs provide unique information on positions and orientations of neighboring protein molecules in the solid phase.

Original languageEnglish (US)
Pages (from-to)17284-17289
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number45
StatePublished - Nov 11 2008


  • Cobalt(II)
  • Matrix metalloproteinase
  • Microcrystal
  • Pseudocontact shift

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