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Updated: Apr 1, 2026
Neutron Crystallography Data Collection and Processing for Modelling Hydrogen Atoms in Protein Structures
Published on: December 1, 2020
Neutron crystallographic studies reveal hydrogen bond and water-mediated interactions between a carbohydrate-binding
S Zoë Fisher1, Laura von Schantz2, Maria Håkansson3
1European Spallation Source , S-221 00 Lund, Sweden.
Abstract:
Carbohydrate-binding modules (CBMs) are key components of many carbohydrate-modifying enzymes. CBMs affect the activity of these enzymes by modulating bonding and catalysis. To further characterize and study CBM-ligand binding interactions, neutron crystallographic studies of an engineered family 4-type CBM in complex with a branched xyloglucan ligand were conducted. The first neutron crystal structure of a CBM-ligand complex reported here shows numerous atomic details of hydrogen bonding and water-mediated interactions and reveals the charged state of key binding cleft amino acid side chains.
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