Ontology highlight
ABSTRACT:
SUBMITTER: Thomas JMH
PROVIDER: S-EPMC5713875 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Thomas Jens M H JMH Simkovic Felix F Keegan Ronan R Mayans Olga O Zhang Chengxin C Zhang Yang Y Rigden Daniel J DJ
Acta crystallographica. Section D, Structural biology 20171122 Pt 12
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 effecti ...[more]