Related Experiment Video
Updated: Sep 27, 2025

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method
Published on: July 27, 2016
Transformation of Chaetomium thermophilum and Affinity Purification of Native Thermostable Protein Complexes
1Biochemistry Center, University of Heidelberg, Heidelberg, Germany.
Abstract:
Chaetomium thermophilum, a eukaryotic thermophile, is an aspiring organism holding great potential for various biochemical and biotechnological applications. Prerequisite for genetic manipulation is a reliable transformation system for target genes combined with selection markers operating at the high growth temperatures of the fungus. Here, we present a detailed protocol for Chaetomium thermophilum protoplast transformation to allow stable chromosomal integration of constructs into its genome, rendering this eukaryotic thermophile a valuable resource for affinity purification of native thermostable protein complexes, like nuclear pore subcomplexes.
More Related Videos
07:01Affinity Purification of Chloroplast Translocon Protein Complexes Using the TAP Tag
Published on: November 1, 2018
14:58Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
Published on: November 12, 2012
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Diversity of Archaea IV
Diversity of Archaea III