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Expression, purification and crystallization of the Cmi immunity protein from Escherichia coli

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Römer,  C
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Patzer,  SI
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Albrecht,  R
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Zeth,  K
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Braun,  V
Department Protein Evolution, Max Planck Institute for Developmental Biology, Max Planck Society;

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Citation

Römer, C., Patzer, S., Albrecht, R., Zeth, K., & Braun, V. (2011). Expression, purification and crystallization of the Cmi immunity protein from Escherichia coli. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67(4), 517-520. doi:10.1107/S1744309111006737.


Cite as: https://hdl.handle.net/21.11116/0000-000A-D8DA-D
Abstract
Many bacteria kill related bacteria by secretion of bacteriocins. In Escherichia coli, the colicin M protein kills E. coli after uptake into the periplasm. Self-protection from destruction is provided by the co-expressed immunity protein. The colicin M immunity protein (Cmi) was cloned, overexpressed and purified to homogeneity. The correct fold of purified Cmi was analyzed by activity tests and circular-dichroism spectroscopy. Crystallization trials yielded crystals, one of which diffracted to a resolution of 1.9 Å in the orthorhombic space group C222(1). The crystal packing, with unit-cell parameters a = 66.02, b = 83.47, c = 38.30 Å, indicated the presence of one monomer in the asymmetric unit with a solvent content of 53%.