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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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.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology, associated group (Burkhard) |
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UniBasel Contributors: | Burkhard, Peter |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Munksgaard |
ISSN: | 0907-4449 |
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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