PMID:21505256
| Citation |
Römer, C, Patzer, SI, Albrecht, R, Zeth, K and Braun, V (2011) Expression, purification and crystallization of the Cmi immunity protein from Escherichia coli. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67:517-20 |
|---|---|
| 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%. |
| Links |
PubMed PMC3080165 Online version:10.1107/S1744309111006737 |
| Keywords |
Colicins/chemistry; Colicins/genetics; Colicins/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Gene Expression |
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