Preliminary X-ray analysis of a new crystal form of recombinant pig kidney DOPA decarboxylase

Malashkevich, V. N. and Burkhard, P. and Dominici, P. and Moore, P. S. and Borri Voltattorni, C. and Jansonius, J. N.. (1999) Preliminary X-ray analysis of a new crystal form of recombinant pig kidney DOPA decarboxylase. Acta Crystallographica. Section D, Biological Crystallography, Vol. 55, Pt. 2. pp. 568-570.

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Official URL: http://edoc.unibas.ch/dok/A5258525

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology, associated group (Burkhard)
UniBasel Contributors:Burkhard, Peter
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:20
Deposited On:22 Mar 2012 13:20

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