Crystallization and preliminary X-ray studies of cold-active protein-tyrosine phosphatase of Shewanella sp.
Cold-active protein-tyrosine phosphatase (PTPase) of Shewanella sp. was expressed, purified and crystallized using the hanging-drop vapour-diffusion method at two different pH values (4.6 and 8.5). Both crystals are orthorhombic and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 56.4, b = 76.8, c = 81.0 A (pH 8.5) and a = 57.1, b = 77.0 and c = 81.5 A (pH 4.6). Diffraction data to 1.82 A for the pH 8.5 crystal and 2.33 A for the pH 4.6 crystal were collected on a multiwire area detector using a rotating-anode X-ray generator.
Laboratory of Biological Chemistry, Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University, Rokkodaicho, Nada-ku, Japan.
Hiroki
H
Tsuruta
Bunzo
B
Mikami
Chiaki
C
Yamamoto
Yasuo
Y
Aizono
D018360:Crystallography, X-Ray; D011487:Protein Conformation; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry*; D020592:Shewanella / Q000201:enzymology*
D017027:Protein Tyrosine Phosphatases