Purification, crystallization and preliminary X-ray crystal structure analysis of copper amine oxidase from Arthrobacter globoformis
- 1 January 1996
- journal article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 52 (1) , 197-198
- https://doi.org/10.1107/s0907444995007529
Abstract
Beta-Phenylethylamine oxidase from the Gram-positive bacterium Arthrobacter globoformis has been crystallized as three crystal forms. Two belong to space group C2 and one to space group P2(1)2(1)2(1), respectively. The unit-cell volumes are consistent with one infunit of 70 644 Da per asymmetric unit for the two monoclinic forms, and with two infunits per asymmetric unit for the orthorhombic crystals. Three-dimensional intensity data have been recorded to 2.8A resolution for one of the monoclinic crystal forms and to 3A, resolution for the orthorhombic crystal form.Keywords
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