Cargando…
Approaches to ab initio molecular replacement of α-helical transmembrane proteins
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 lib...
Autores principales: | Thomas, Jens M. H., Simkovic, Felix, Keegan, Ronan, Mayans, Olga, Zhang, Chengxin, Zhang, Yang, Rigden, Daniel J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5713875/ https://www.ncbi.nlm.nih.gov/pubmed/29199978 http://dx.doi.org/10.1107/S2059798317016436 |
Ejemplares similares
-
Residue contacts predicted by evolutionary covariance extend the application of ab initio molecular replacement to larger and more challenging protein folds
por: Simkovic, Felix, et al.
Publicado: (2016) -
Exploring the speed and performance of molecular replacement with AMPLE using QUARK ab initio protein models
por: Keegan, Ronan M., et al.
Publicado: (2015) -
Ensembles generated from crystal structures of single distant homologues solve challenging molecular-replacement cases in AMPLE
por: Rigden, Daniel J., et al.
Publicado: (2018) -
Helical ensembles outperform ideal helices in molecular replacement
por: Sánchez Rodríguez, Filomeno, et al.
Publicado: (2020) -
Ab initio molecular-replacement phasing for symmetric helical membrane proteins
por: Strop, Pavel, et al.
Publicado: (2007)