CRYSTALLIZATION AND PRELIMINARY-X-RAY DIFFRACTION STUDIES OF THE OXYGENATING SUBUNIT OF 3,6-DIKETOCAMPHANE MONOOXYGENASE FROM PSEUDOMONAS-PUTIDA

The oxygenating constituent of the 3,6-diketocamphane monooxygenase is ozyme from Pseudomonas putida NCIMB 10007 has been crystallized under two different conditions. Crystals were initially grown from polyethyl ene glycol (PEG) 8000 and sodium acetate using the vapour-phase diffus ion method. The crystals were of orthorhombic P2(1)2(1)2(1) space grou p, with cell dimensions a = 55.8, b = 94.5 and c = 163.7 Angstrom and diffracted to 2.8 Angstrom resolution. More recently, improved crystal s, which diffracted beyond 2 Angstrom, have been grown from ammonium s ulfate. These crystals also belong to the orthorhombic P2(1)2(1)2(1) s pace group. with cell dimensions of a = 54.6, b = 93.2 and c = 154.1 A ngstrom. A full native data set to 2.5 Angstrom resolution has been co llected from the ammonium sulfate grown crystals.