Expression, purification and crystallisation of phosphorylase kinase catalytic domain.

@article{Owen1995ExpressionPA,
  title={Expression, purification and crystallisation of phosphorylase kinase catalytic domain.},
  author={David J. Owen and Anastassios C Papageorgiou and Elspeth F. Garman and Mark E. Noble and Louise N. Johnson},
  journal={Journal of molecular biology},
  year={1995},
  volume={246 3},
  pages={
          374-81
        }
}
The catalytic subunit of phosphorylase kinase is composed of a kinase catalytic core domain (residues 1 to 298), which has a 33% identity with the kinase core of the cyclic AMP-dependent protein kinase, and a C-terminal calmodulin binding domain. The kinase domain of the catalytic subunit has been expressed in Escherichia coli, purified and crystallised in the presence of ATP and magnesium from 5% (w/v) polyethylene glycol 8000, 10% (v/v) glycerol, 50 mM Hepes/NaOH (pH 6.9). A three-fold excess… CONTINUE READING

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