Crystallisation and characterisation of muscle proteins: a mini-review.
Crystallisation
Muscle proteins
Myosin-binding protein-C
X-ray crystallography
α-actinin
Journal
Journal of muscle research and cell motility
ISSN: 1573-2657
Titre abrégé: J Muscle Res Cell Motil
Pays: Netherlands
ID NLM: 8006298
Informations de publication
Date de publication:
09 2023
09 2023
Historique:
received:
27
09
2022
accepted:
29
03
2023
medline:
2
10
2023
pubmed:
3
5
2023
entrez:
3
5
2023
Statut:
ppublish
Résumé
The techniques of X-ray protein crystallography, NMR and high-resolution cryo-electron microscopy have all been used to determine the high-resolution structure of proteins. The most-commonly used method, however, remains X-ray crystallography but it does rely heavily on the production of suitable crystals. Indeed, the production of diffraction quality crystals remains the rate-limiting step for most protein systems. This mini-review highlights the crystallisation trials that used existing and newly developed crystallisation methods on two muscle protein targets - the actin binding domain (ABD) of α-actinin and the C0-C1 domain of human cardiac myosin binding protein C (cMyBP-C). Furthermore, using heterogenous nucleating agents the crystallisation of the C1 domain of cMyBP-C was successfully achieved in house along with preliminary actin binding studies using electron microscopy and co-sedimentation assays .
Identifiants
pubmed: 37133758
doi: 10.1007/s10974-023-09648-2
pii: 10.1007/s10974-023-09648-2
pmc: PMC10542657
doi:
Substances chimiques
Actins
0
Muscle Proteins
0
Actinin
11003-00-2
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
209-215Subventions
Organisme : British Heart Foundation
Pays : United Kingdom
Informations de copyright
© 2023. The Author(s).
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