Preliminary investigation of crystals of lipase I from Rhizopus niveus.
Lipase I from Rhizopus niveus consists of two polypeptide chains bound non-covalently. Lipase I has been crystallized in a form suitable for X-ray diffraction analysis using the hanging drop method of vapour diffusion at 20 degrees C. The crystals grew at pH 6.0 to 7.0 using 14 to 16% polyethylene glycol 8000 as the precipitant. The crystals are tetragonal with space group P4(1) (or P4(3)) and cell dimensions of a = b = 83.7 A, c = 137.9 A. There are two protein molecules in the asymmetric unit. The diffraction pattern extends to at least 2.5 A resolution.
Kohno
M
M
Central Research Institute Tsukuba R&D Center, Fuji Oil Co., Ltd, Ibaraki, Japan.
Kugimiya
W
W
Hashimoto
Y
Y
Morita
Y
Y
D008049:Lipase / Q000737:chemistry*; D012233:Rhizopus / Q000201:enzymology*; D014961:X-Ray Diffraction
D008049:Lipase