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

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 55; no. 2; pp. 568 - 570
• Main Authors: Malashkevich, V. N., Burkhard, P., Dominici, P., Moore, P. S., Borri Voltattorni, C., Jansonius, J. N.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.02.1999
• Subjects: Animals; Crystallography, X-Ray; DOPA decarboxylase; Dopa Decarboxylase - chemistry; Kidney - enzymology; Protein Conformation; Recombinant Proteins - chemistry; Swine
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444998006283

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 Å. Both the self‐rotation function and the good diffraction quality of these crystals (2.5 Å 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.