English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
/persons/resource/persons275406

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

/persons/resource/persons275402

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

/persons/resource/persons77670

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

/persons/resource/persons78923

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

/persons/resource/persons271640

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

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
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%.