Approaches to ab initio molecular replacement of α-helical transmembrane proteins

Thomas, Jens MH ORCID: 0000-0003-0277-8505, Simkovic, Felix ORCID: 0000-0003-3430-6828, Keegan, Ronan, Mayans, Olga, Zhang, Chengxin, Zhang, Yang and Rigden, Daniel J ORCID: 0000-0002-7565-8937 (2017) Approaches to ab initio molecular replacement of α-helical transmembrane proteins. Acta Crystallographica Section D: Structural Biology, 73 (12). pp. 985-996.

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Official URL: http://scripts.iucr.org/cgi-bin/paper?S20597983170...

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.

Item Type:	Article
Uncontrolled Keywords:	transmembrane proteins, ab initio phasing, ab initio modelling, predicted contacts
Depositing User:	Symplectic Admin
Date Deposited:	12 Jan 2018 10:18
Last Modified:	19 Jan 2023 06:45
DOI:	10.1107/S2059798317016436
Open Access URL:	https://journals.iucr.org/d/issues/2017/12/00/qh50...
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3015916