Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions.

Heterologous expression of mycobacterial Esx complexes in Escherichia coli for structural studies is facilitated by the use of maltose binding protein fusions.

The expression of heteroligomeric protein complexes for structural studies often requires a special coexpression strategy. The reason is that the solubility and proper folding of each subunit of the complex requires physical association with other subunits of the complex. The genomes of pathogenic m...

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Bibliographic Details
Main Authors: Mark A Arbing, Sum Chan, Liam Harris, Emmeline Kuo, Tina T Zhou, Christine J Ahn, Lin Nguyen, Qixin He, Jamie Lu, Phuong T Menchavez, Annie Shin, Thomas Holton, Michael R Sawaya, Duilio Cascio, David Eisenberg
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3843698?pdf=render

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