Abstract

DOPA decarboxylase is responsible for the synthesis of the key neurotransmitters dopamine and serotonin via decarboxylation of L-3, 4-dihydroxyphenylalanine (L-DOPA) and L-5-hydroxytryptophan, respectively. The crystals of recombinant DOPA decarboxylase differ from those previously reported for the enzyme purified from pig kidney. They belong to space group P622 with unit-cell dimensions a = b = 302.6, c = 178.1 A. Both the self-rotation function and the good diffraction quality of these crystals (2.5 A on a synchrotron source) suggest that there should be at least three protein dimers in the asymmetric unit. Diffraction data sets have been collected for the native enzyme and a heavy-atom derivative.

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