Crystallization and preliminary X-ray studies of methyl parathion hydrolase from Pseudomonas sp. WBC-3.
Methyl parathion hydrolase (MPH) from Pseudomonas sp. WBC-3, an enzyme that catalyzes the degradation of methyl parathion (O,O-dimethyl O-p-nitrophenyl phosphorothioate; MP), has been purified and crystallized by the hanging-drop vapour-diffusion method. The crystals were grown at 291 K using a precipitant solution consisting of 30% PEG 400, 0.1 M sodium acetate pH 4.6, 0.1 M CdCl(2). MPH is a zinc-containing enzyme judged by inductively coupled plasma mass-spectrometric (ICP-MS) analysis. Multiple-wavelength anomalous dispersive X-ray data were collected at 2.5 A resolution from a single crystal on beamline 41XU at SPring-8. The crystal belongs to space group P4(3)2(1)2, with unit-cell parameters a = 84.94, b = 84.94, c = 200.38 A, alpha = beta = gamma = 90 degrees. The asymmetric unit contains two molecules and has a solvent content of approximately 52%. Crystal structure determination is in progress.
Sun
Lei
L
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Science and Laboratory of Structural Biology, Tsinghua University, Beijing, People's Republic of China.
Dong
Yanjie
Y
Zhou
Yafeng
Y
Yang
Maojun
M
Zhang
Chenggang
C
Rao
Zihe
Z
Zhang
Xian-en
XE
D003460:Crystallization; D018360:Crystallography, X-Ray; D008743:Methyl Parathion / Q000378:metabolism*; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*
D008743:Methyl Parathion; C495424:methyl parathion hydrolase, Pseudomonas; D010744:Phosphoric Monoester Hydrolases