Crystallization and initial spectroscopic characterization of the heme-containing dehaloperoxidase from the marine polychaete Amphitrite ornata

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 52; no. 6; pp. 1191 - 1193
• Main Authors: Zhang, E., Chen, Y. P., Roach, M. P., Lincoln, D. E., Lovell, C. R., Woodin, S. A., Dawson, J. H., Lebioda, L.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.11.1996
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S0907444996007974

The heme‐containing dehaloperoxidase from Amphitrite ornata was crystallized from an unbuffered solution containing 30% PEG 8000 and 200 mM ammonium sulfate by the hanging‐drop vapor‐diffusion method. Dark‐red bipyramidal crystals are orthorhombic in space group P212121 with unit‐cell dimensions a = 68.5, b = 68.4 and c = 61.1 Å. The asymmetric unit contains two subunits related by a non‐crystallographic twofold axis. The crystals scatter beyond 2 Å resolution. The native data have been collected and one single‐site mercury derivative has been found. SIRAS phasing was used to determine the positions of the heme Fe atoms and structure determination is in progress. A preliminary spectroscopic investigation indicates that the heme is protoporphyrin IX and its coordination sphere resembles that of a typical heme peroxidase, i.e. histidine ligated. Detailed spectroscopic and electrochemical studies are now under way.