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Crystallization and crystal data on tyrosine phenol-lyase.

T V Demidkina1, I V Myagkikh, A A Antson

  • 1Institute of Molecular Biology, USSR Academy of Sciences, Moscow.

FEBS Letters
|May 23, 1988
PubMed
Summary

Crystallization of tyrosine phenol-lyase, a pyridoxal 5'-phosphate-dependent enzyme, was achieved. This provides a foundation for structural studies of this important biocatalyst.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Tyrosine phenol-lyase (EC 4.1.99.2) is a pyridoxal 5 -phosphate-dependent enzyme.
  • This enzyme from Citrobacter intermedius plays a role in amino acid metabolism.

Purpose of the Study:

  • To obtain crystals of the apoenzyme of tyrosine phenol-lyase suitable for X-ray diffraction analysis.
  • To characterize the crystallographic properties of the enzyme.

Main Methods:

  • Protein crystallization using vapor diffusion.
  • X-ray diffraction to determine crystal parameters and resolution.
  • Preparation of heavy-atom derivatives.

Main Results:

  • Crystals of tyrosine phenol-lyase apoenzyme were successfully grown.

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  • The crystals belong to space group P2(1)2(1)2 with unit cell dimensions a = 75.5 A, b = 138.4 A, c = 94.1 A.
  • Diffraction data were collected to 2.7 A resolution, and two heavy-atom derivatives were obtained.

    • Conclusions:

    • The successful crystallization and initial characterization of tyrosine phenol-lyase apoenzyme crystals.
    • These crystals are suitable for further structural determination using X-ray crystallography.
    • The obtained heavy-atom derivatives will aid in solving the phase problem for structure determination.