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Crystallization and crystal data on tyrosine phenol-lyase

Research output: Contribution to journalArticle

Author(s)

  • T V Demidkina
  • I V Myagkikh
  • A A Antson
  • E H Harutyunyan

Department/unit(s)

Publication details

JournalFEBS Letters
DatePublished - 23 May 1988
Issue number2
Volume232
Number of pages2
Pages (from-to)381-2
Original languageEnglish

Abstract

Crystals of the apoenzyme of tyrosine phenol-lyase (EC 4.1.99.2), a pyridoxal 5'-phosphate-dependent enzyme from Citrobacter intermedius, have been grown by vapor diffusion of an ammonium sulfate solution to a protein solution. The crystals belong to space group P2(1)2(1)2, with dimensions of a = 75.5 A, b = 138.4 A and c = 94.1 A and diffract up to 2.7 A resolution. The asymmetric unit contains one half of the enzyme tetrameric molecule. Two heavy-atom derivatives of the crystals have been obtained.

    Research areas

  • Ammonium Sulfate, Apoenzymes, Apoproteins, Chemical Precipitation, Citrobacter, Crystallization, Hydrogen-Ion Concentration, Lyases, Macromolecular Substances, Polyethylene Glycols, Tyrosine Phenol-Lyase, X-Ray Diffraction

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