CRYSTALLIZATION AND PRELIMINARY-X-RAY STUDIES OF RECOMBINANT HORSERADISH-PEROXIDASE

A non-glycosylated form of horseradish peroxidase c extracted from Esc herichia coli inclusion bodies and refolded in the presence of haem an d Ca2+ ions has been used to grow protein crystals suitable for X-ray diffraction analysis. The crystals are prisms in the trigonal space gr oup P3(1)12 or P3(2)12 with a = b = 158.9 and c = 114.3 Angstrom and d iffract to 1.9 Angstrom. There are four molecules, each of 34 kDa, in the asymmetric unit. The molecules of the asymmetric unit are related by approximate translational symmetry, resulting in pseudo-centerings. Data to approximately 15 Angstrom can thus be described by a lattice of a' = b' = 91.7 Angstrom and c' = 57.1 Angstrom, alpha = beta = 90 d egrees and gamma = 120 degrees, including four molecules.