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

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

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Bibliographic Details
Published in:Biomolecular NMR assignments 2019-04, Vol.13 (1), p.55-58
Main Authors: Madland, Eva, Kitaoku, Yoshihito, Sætrom, Gerd Inger, Leth, Maria Louise, Ejby, Morten, Hachem, Maher Abou, Aachmann, Finn Lillelund
Format: Article
Language:English
Subjects:
Biochemistry
Biological and Medical Physics
Biophysics
Glycoside hydrolase
Hydrolase
NMR
Nuclear magnetic resonance
Physics
Physics and Astronomy
Polymer Sciences
Roseburia intestinalis
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Summary:The N-terminal domain (residues 28–165) from the glycoside hydrolase family 10 from Roseburia intestinalis ( Ri CBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli . Here we report 1 H, 13 C and 15 N NMR chemical shift assignments for this carbohydrate binding module (CBM).
ISSN:1874-2718
1874-270X
DOI:10.1007/s12104-018-9850-3