Neutron crystallographic refinement with REFMAC5 from the CCP4 suite.
CCP4
H atoms
REFMAC5
crystallographic refinement
neutron macromolecular crystallography
Journal
Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043
Informations de publication
Date de publication:
01 Dec 2023
01 Dec 2023
Historique:
received:
06
08
2023
accepted:
05
10
2023
medline:
5
12
2023
pubmed:
3
11
2023
entrez:
3
11
2023
Statut:
ppublish
Résumé
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 (
Identifiants
pubmed: 37921806
pii: S2059798323008793
doi: 10.1107/S2059798323008793
doi:
Substances chimiques
Proteins
0
Deuterium
AR09D82C7G
Hydrogen
7YNJ3PO35Z
Macromolecular Substances
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1056-1070Subventions
Organisme : Medical Research Council
ID : MC_UP_A025_1012
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/P000169/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/S007083/1
Pays : United Kingdom
Informations de copyright
open access.