Datta, Ajit B. ; Chakrabarti, Pinak ; Subramanya, H. S. ; Parrack, Pradeep (2001) Purification and crystallization of CII: an unstable transcription activator from phage λ Biochemical and Biophysical Research Communications, 288 (4). pp. 997-1000. ISSN 0006-291X
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00062...
Related URL: http://dx.doi.org/10.1006/bbrc.2001.5880
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 Å and belong to the space group C222 with unit-cell parameters a = 64.10, b = 106.95 and c = 120.16 Å.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Bacteriophage Lambda; CII Protein; Crystallization; Lysogeny; Genetic Switch |
| ID Code: | 21459 |
| Deposited On: | 22 Nov 2010 11:20 |
| Last Modified: | 20 May 2011 10:23 |
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