Crystallization and preliminary X-ray analysis of phenol hydroxylase from Trichosporon cutaneum.
Recombinant phenol hydroxylase from the soil yeast Trichosporon cutaneum has been crystallized with PEG 4000 as precipitant. The crystals are monoclinic, space group P2(1) with cell dimensions a = 101.8 A, b = 153.0 A, c = 116.0 A and beta = 114.8 degrees. The crystal asymmetric unit most likely contains two dimers of phenol hydroxylase corresponding to a packing density in the crystals of 2.54 A 3/Da. The self-rotation function is consistent with the packing of two dimers in the asymmetric unit. The observed diffraction pattern extends beyond 2.8 A resolution and the crystals are well suited for structural analysis by X-ray diffraction methods.
Enroth
C
C
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala.
Huang
W
W
Waters
S
S
Neujahr
H
H
Lindqvist
Y
Y
Schneider
G
G
D003460:Crystallization; D018360:Crystallography, X-Ray; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000302:isolation & purification*; D014250:Trichosporon / Q000201:enzymology*
D006899:Mixed Function Oxygenases; C022336:phenol 2-monooxygenase