Purification and crystallization of CII: an unstable transcription activator from phage lambda
| Autor: | Pradeep Parrack, Pinak Chakrabarti, Ajit B. Datta, H.S. Subramanya |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Biophysics
medicine.disease_cause Biochemistry law.invention Bacteriophage Viral Proteins Tetramer X-Ray Diffraction law Lysogenic cycle medicine Native state Molecular Biology Gene Escherichia coli chemistry.chemical_classification biology Cell Biology biology.organism_classification Bacteriophage lambda Amino acid chemistry Recombinant DNA Thermodynamics Electrophoresis Polyacrylamide Gel Crystallization Transcription Factors |
| Zdroj: | Biochemical and biophysical research communications. 288(4) |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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