Neutron crystallographic refinement with REFMAC5 from the CCP4 suite.

ABSTRACT: Hydrogen (H) atoms are abundant in macromolecules and often play critical roles in enzyme catalysis, ligand-recognition processes and protein-protein interactions. However, their direct visualization by diffraction techniques is challenging. Macromolecular X-ray crystallography affords the localization of only the most ordered H atoms at (sub-)atomic resolution (around 1.2 Å or higher). However, many H atoms of biochemical significance remain undetectable by this method. In contrast, neutron diffraction methods enable the visualization of most H atoms, typically in the form of deuterium (²H) atoms, at much more common resolution values (better than 2.5 Å). Thus, neutron crystallography, although technically demanding, is often the method of choice when direct information on prot

SUBMITTER: Catapano L 

PROVIDER: S-EPMC7615533 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature