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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase.

A protein phosphatase (PPase) from the bacteriophage lambda was overexpressed in Escherichia coli. The recombinant enzyme was purified to homogeneity yielding approximately 17 mg of enzyme from a single liter of bacterial culture. Biochemical characterization of the enzyme showed that it required Mn2+ or Ni2+ as an activator. The recombinant enzyme was active toward serine, threonine, and tyrosine phosphoproteins and phosphopeptides. Surprisingly, the bacterial histidyl phosphoprotein, NRII, was also dephosphorylated by the lambda-PPase. The lambda-PPase shares a number of kinetic and structural properties with the eukaryotic Ser/Thr phosphatases, suggesting that the lambda-PPase will serve as a good model for structure-function studies. Crystallization of the recombinant purified lambda-PPase yielded monoclinic crystals. The crystals diffract to 4.0 A when exposed to synchrotron x-ray radiation.[1]

References

  1. Expression, purification, crystallization, and biochemical characterization of a recombinant protein phosphatase. Zhuo, S., Clemens, J.C., Hakes, D.J., Barford, D., Dixon, J.E. J. Biol. Chem. (1993) [Pubmed]
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