Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement.
X-ray/neutron joint refinement
copper amine oxidases
neutron crystallography
quinone cofactor
Journal
IUCrJ
ISSN: 2052-2525
Titre abrégé: IUCrJ
Pays: England
ID NLM: 101623101
Informations de publication
Date de publication:
01 May 2022
01 May 2022
Historique:
received:
02
02
2022
accepted:
01
04
2022
entrez:
13
5
2022
pubmed:
14
5
2022
medline:
14
5
2022
Statut:
epublish
Résumé
Protein neutron crystallography is a powerful technique to determine the positions of H atoms, providing crucial biochemical information such as the protonation states of catalytic groups and the geometry of hydrogen bonds. Recently, the crystal structure of a bacterial copper amine oxidase was determined by joint refinement using X-ray and neutron diffraction data sets at resolutions of 1.14 and 1.72 Å, respectively [Murakawa
Identifiants
pubmed: 35546796
doi: 10.1107/S2052252522003657
pii: S2052252522003657
pmc: PMC9067118
doi:
Types de publication
Journal Article
Langues
eng
Pagination
342-348Informations de copyright
© Takeshi Murakawa et al. 2022.
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