The accuracy of protein models automatically built into cryo-EM maps with ARP/wARP.
Acta Crystallogr D Struct Biol
; 77(Pt 2): 142-150, 2021 Feb 01.
Article
en En
| MEDLINE
| ID: mdl-33559604
ABSTRACT
Recent developments in cryogenic electron microscopy (cryo-EM) have enabled structural studies of large macromolecular complexes at resolutions previously only attainable using macromolecular crystallography. Although a number of methods can already assist in de novo building of models into high-resolution cryo-EM maps, automated and reliable map interpretation remains a challenge. Presented here is a systematic study of the accuracy of models built into cryo-EM maps using ARP/wARP. It is demonstrated that the local resolution is a good indicator of map interpretability, and for the majority of the test cases ARP/wARP correctly builds 90% of main-chain fragments in regions where the local resolution is 4.0â
Å or better. It is also demonstrated that the coordinate accuracy for models built into cryo-EM maps is comparable to that of X-ray crystallographic models at similar local cryo-EM and crystallographic resolutions. The model accuracy also correlates with the refined atomic displacement parameters.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas
/
Microscopía por Crioelectrón
/
Sustancias Macromoleculares
Idioma:
En
Revista:
Acta Crystallogr D Struct Biol
Año:
2021
Tipo del documento:
Article
País de afiliación:
Alemania