Approaches to ab initio molecular replacement of α-helical transmembrane proteins.
Acta Crystallogr D Struct Biol
; 73(Pt 12): 985-996, 2017 Dec 01.
Article
en En
| MEDLINE
| ID: mdl-29199978
ABSTRACT
α-Helical transmembrane proteins are a ubiquitous and important class of proteins, but present difficulties for crystallographic structure solution. Here, the effectiveness of the AMPLE molecular replacement pipeline in solving α-helical transmembrane-protein structures is assessed using a small library of eight ideal helices, as well as search models derived from ab initio models generated both with and without evolutionary contact information. The ideal helices prove to be surprisingly effective at solving higher resolution structures, but ab initio-derived search models are able to solve structures that could not be solved with the ideal helices. The addition of evolutionary contact information results in a marked improvement in the modelling and makes additional solutions possible.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Membrana Celular
/
Conformación Proteica en Hélice alfa
/
Proteínas de la Membrana
Tipo de estudio:
Prognostic_studies
Límite:
Humans
Idioma:
En
Revista:
Acta Crystallogr D Struct Biol
Año:
2017
Tipo del documento:
Article
País de afiliación:
Reino Unido