type	Journal Article
authors	Malashkevich, V. N.; Burkhard, P.; Dominici, P.; Moore, P. S.; Borri Voltattorni, C.; Jansonius, J. N.
title	Preliminary X-ray analysis of a new crystal form of recombinant pig kidney DOPA decarboxylase
journal	Acta Crystallogr D Biol Crystallogr
Activity	4.1.1.28
ui	99190927
year	(1999)
volume	55
number	Pt 2
pages	568-70.
keywords	Animal
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.
last changed	2002/11/12 16:17