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Updated: Feb 27, 2026

The MultiBac Protein Complex Production Platform at the EMBL

The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

Large Complexes: Cloning Strategy, Production, and Purification.

Eric Durand¹, Roland Lloubes²

¹Laboratoire d'Ingénierie des Systèmes Macromoléculaires (LISM, UMR7255), Institut de Microbiologie de la Méditerranée (IMM), Aix-Marseille Univ and CNRS, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France.

Methods in Molecular Biology (Clifton, N.J.)

|July 2, 2017

Summary

This summary is machine-generated.

Researchers developed cloning and purification methods for bacterial membrane protein complexes. This work focuses on the Type VI secretion TssJLM complex in Escherichia coli, aiding future structural and functional studies.

Keywords:

Escherichia coli Membrane protein complexes Protein purification T7 overexpression

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Last Updated: Feb 27, 2026

The MultiBac Protein Complex Production Platform at the EMBL

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Area of Science:

Molecular biology
Structural biology
Microbiology

Background:

Membrane proteins form essential complexes in the cell envelope of Gram-negative bacteria.
Few atomic structures exist for these large, multi-protein molecular machines, hindering functional understanding.
Dedicated production and purification strategies are crucial for studying these complexes.

Purpose of the Study:

To present cloning procedures for overproducing membrane proteins in Escherichia coli.
To describe a cloning and purification strategy for the Type VI secretion TssJLM membrane complex.

Main Methods:

Cloning procedures for overproduction of membrane proteins in Escherichia coli.
Specific cloning and purification strategy development for the TssJLM complex.

Main Results:

Established methods for overproducing membrane proteins in E. coli.
Successfully developed a cloning and purification strategy for the TssJLM membrane complex.

Conclusions:

The presented methods facilitate the study of complex membrane protein assemblies.
This work provides a foundation for future structural and functional investigations of the Type VI secretion system.