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 isozyme from Pseudomonas putida NCIMB 10007 has been crystallized under two different conditions. Crystals were initially grown from polyethylene glycol (PEG) 8000 and sodium acetate using the vapour-phase diffusion method. The crystals were of orthorhombic P212121 space group, with cell dimensions a = 55.8, b = 94.5 and c = 163.7 A and diffracted to 2.8 A resolution. More recently, improved crystals, which diffracted beyond 2 A, have been grown from ammonium sulfate. These crystals also belong to the orthorhombic P212121 space group, with cell dimensions of a = 54.6, b = 93.2 and c = 154. 1 A. A full native data set to 2.5 A resolution has been collected from the ammonium sulfate grown crystals.
Departments of Chemistry and Biological Sciences, University of Exeter, Exeter EX4 4QD, England.
E J
EJ
McGhie
M N
MN
Isupov
E
E
Schröder
J A
JA
Littlechild
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002164:Camphor / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D010105:Oxygenases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000201:enzymology*
D001426:Bacterial Proteins; D002164:Camphor; D010105:Oxygenases; C115882:3,6-diketocamphane monooxygenase