1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis

Eva Madland, Yoshihito Kitaoku, Gerd Inger Sætrom, Maria Louise Leth, Morten Ejby, Maher Abou Hachem, Finn Lillelund Aachmann

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

The N-terminal domain (residues 28-165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report 1H, 13C and 15N NMR chemical shift assignments for this carbohydrate binding module (CBM).

Original languageEnglish
Pages (from-to)55-58
Number of pages4
JournalBiomolecular NMR Assignments
Volume13
Issue number1
DOIs
Publication statusPublished - Apr 2019
Externally publishedYes

Keywords

  • Carbon Isotopes
  • Endo-1,4-beta Xylanases/chemistry
  • Firmicutes/enzymology
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary
  • Protons
  • Receptors, Cell Surface/chemistry

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