| Literature DB >> 34458442 |
Yung-Ning Chang1, Farooque R Shaik2, Yvonne Neldner3, Eric R Geertsma1.
Abstract
The SLC26 or SulP proteins constitute a large family of anion transporters that are ubiquitously expressed in pro- and eukaryotes. In human, SLC26 proteins perform important roles in ion homeostasis and malfunctioning of selected members is associated with diseases. This protocol details the production and crystallization of a prokaryotic SLC26 homolog, termed SLC26Dg, from Deinococcus geothermalis. Following these instructions we obtained well-folded and homogenous material of the membrane protein SLC26Dg and the nanobody Nb5776 that enabled us to crystallize the complex and determine its structure ( Geertsma et al., 2015 ). The procedure may be adapted to purify and crystallize other membrane protein complexes.Entities:
Keywords: Crystallization chaperone; Membrane transport protein; Nanobody; SLC26; Solute carrier
Year: 2017 PMID: 34458442 PMCID: PMC8376587 DOI: 10.21769/BioProtoc.2116
Source DB: PubMed Journal: Bio Protoc ISSN: 2331-8325