|
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 |
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