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
em 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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Membrana Celular
/
Conformação Proteica em alfa-Hélice
/
Proteínas de Membrana
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article