Vn. Malashkevich et al., Preliminary X-ray analysis of a new crystal form of recombinant pig kidneyDOPA decarboxylase, ACT CRYST D, 55, 1999, pp. 568-570
DOPA decarboxylase is responsible for the synthesis of the key neurotransmi
tters dopamine and serotonin via decarboxylation of L-3,4-dihydroxyphenylal
anine (L-DOPA) and L-5-hydroxytryptophan, respectively. The crystals of rec
ombinant DOPA decarboxylase differ from those previously reported for the e
nzyme purified from pig kidney. They belong to space group P622 with unit-c
ell dimensions a = b = 302.6, c = 178.1 Angstrom. Both the self-rotation fu
nction and the good diffraction quality of these crystals (2.5 Angstrom on
a synchrotron source) suggest that there should be at least three protein d
imers in the asymmetric unit. Diffraction data sets have been collected for
the native enzyme and a heavy-atom derivative.