PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF MANGANESE PEROXIDASE FROM PHANEROCHAETE-CHRYSOSPORIUM

Manganese peroxidase from the white rot basidiomycete Phanerochaete chrysosporium has been crystallized in a form suitable for high-resolution X-ray structure determination. Crystals were grown from solutions containing 30% polyethylene glycol 8000, ammonium sulfate and cacodylate buffer at pH 6.5, using macroseeding techniques. A complete data set has been obtained to 2.06 Å resolution. The data can be indexed in space group P1 with a = 45·96 Å, b = 53·77 Å, c = 84·87 Å, ± = 97·01°, ² = 105·72° and ³= 90·1°, with two peroxidase molecules per asymmetric unit, or in space group C2 with a = 163·23 Å, b = 45·97 Å, c = 53·72 Å and ² = 97·16°, with only one molecule in the assymetric unit. Lignin peroxidase, which shares about 57% sequence identity with manganese peroxidase, was used as a probe for molecular replacement. Unique rotation and translation solutions have been obtained in space groups P1 and C2. The structure has been partially refined in space group C2 to R = 0·22 for data between 10 and 2.06 Å. © 1994 Academic Press Limited.