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

J Mol Biol. 1994 Nov 11;243(5):947-9. doi: 10.1006/jmbi.1994.1695.

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 A, b = 69.3 A, c = 123.7 A 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 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallization
  • Ethylenes / biosynthesis
  • Fruit / enzymology*
  • Lyases / chemistry*
  • Recombinant Proteins / chemistry
  • X-Ray Diffraction

Substances

  • Ethylenes
  • Recombinant Proteins
  • ethylene
  • Lyases
  • 1-aminocyclopropanecarboxylate synthase