Oxygen-Sensitive Metalloprotein Structure Determination by Cryo-Electron Microscopy.
anaerobic environment
cryo-electron microscopy
iron-sulfur cluster
metalloproteins
Journal
Biomolecules
ISSN: 2218-273X
Titre abrégé: Biomolecules
Pays: Switzerland
ID NLM: 101596414
Informations de publication
Date de publication:
12 03 2022
12 03 2022
Historique:
received:
26
01
2022
revised:
07
03
2022
accepted:
10
03
2022
entrez:
25
3
2022
pubmed:
26
3
2022
medline:
30
4
2022
Statut:
epublish
Résumé
Metalloproteins are involved in key cell processes such as photosynthesis, respiration, and oxygen transport. However, the presence of transition metals (notably iron as a component of [Fe-S] clusters) often makes these proteins sensitive to oxygen-induced degradation. Consequently, their study usually requires strict anaerobic conditions. Although X-ray crystallography has been the method of choice for solving macromolecular structures for many years, recently electron microscopy has also become an increasingly powerful structure-solving technique. We have used our previous experience with cryo-crystallography to develop a method to prepare cryo-EM grids in an anaerobic chamber and have applied it to solve the structures of apoferritin and the 3 [Fe
Identifiants
pubmed: 35327633
pii: biom12030441
doi: 10.3390/biom12030441
pmc: PMC8945911
pii:
doi:
Substances chimiques
Metalloproteins
0
Apoferritins
9013-31-4
Oxygen
S88TT14065
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
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