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Updated: Oct 22, 2025

Author Spotlight: Expression and Purification of Human Solute Carrier Transporters Using Codon-Optimized Genes
Published on: September 29, 2023
Production, Purification and Crystallization of a ProkaryoticSLC26 Homolog for Structural Studies
Yung-Ning Chang1, Farooque R Shaik2, Yvonne Neldner3
1Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Frankfurt am Main, Germany.
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.

