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.
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.
Hohenester
E
E
Department of Structural Biology Biozentrum, University of Basel, Switzerland.
White
M F
MF
Kirsch
J F
JF
Jansonius
J N
JN
D003460:Crystallization; D005030:Ethylenes / Q000096:biosynthesis; D005638:Fruit / Q000201:enzymology*; D008190:Lyases / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D014961:X-Ray Diffraction
D005030:Ethylenes; D011994:Recombinant Proteins; C036216:ethylene; D008190:Lyases; C021773:1-aminocyclopropanecarboxylate synthase