CRYSTALLIZATION AND PRELIMINARY-X-RAY ANALYSIS OF RECOMBINANT 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE FROM APPLE - A KEY ENZYME IN THE BIOSYNTHESIS OF THE PLANT HORMONE ETHYLENE

E HOHENESTER, Malcolm F White, J F KIRSCH, J N JANSONIUS

Research output: Contribution to journalComment/debatepeer-review

7 Citations (Scopus)

Abstract

Crystals of recombinant 1-aminocyclopropane-1-carboxylate synthase from apple have been obtained with polyethylene glycol as precipitant using a combination of vapour diffusion and macroseeding techniques. The crystals are of space group P2(1), with unit-cell constants a = 53.7 Angstrom, b = 69.3 Angstrom, c = 123.7 Angstrom and beta = 89.9 degrees. The asymmetric unit content is a 1-aminocyclopropane-1-carboxylate synthase dimer with a molecular mass of 94 kDa. Diffraction extends to 2.2 Angstrom resolution.

Original languageEnglish
Pages (from-to)947-949
Number of pages3
JournalJournal of Molecular Biology
Volume243
Issue number5
Publication statusPublished - 11 Nov 1994

Keywords

  • ETHYLENE BIOSYNTHESIS
  • PYRIDOXAL-5'-PHOSPHATE
  • CRYSTALLIZATION
  • MACROSEEDING
  • X-RAY CRYSTALLOGRAPHY
  • PROTEINS
  • FRUIT

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