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  • Title: Purification and crystallization of CII: an unstable transcription activator from phage lambda.
    Author: Datta AB, Chakrabarti P, Subramanya HS, Parrack P.
    Journal: Biochem Biophys Res Commun; 2001 Nov 09; 288(4):997-1000. PubMed ID: 11689008.
    Abstract:
    The CII protein of the temperate bacteriophage lambda is a transcriptional activator involved in the lysis-lysogeny switch of the phage. It is an unstable protein of 97 amino acids and is known to exist as a tetramer in the native state. The cII gene has been cloned and expressed in Escherichia coli using a T7 promoter based over-expression system. The recombinant CII protein has been purified to homogeneity by ammonium sulfate fractionation followed by two steps of ion-exchange chromatography. The purified protein crystallized at pH 8.2 in hanging-drop vapor diffusion method at 293 K. The crystals diffract to a resolution of 2.8 A and belong to the space group C222 with unit-cell parameters a = 64.10, b = 106.95 and c = 120.16 A.
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