Extracellular overproduction and preliminary crystallographic analysis of a family I.3 lipase.
A family I.3 lipase from Pseudomonas sp. MIS38 was secreted from Escherichia coli cells to the external medium, purified and crystallized and preliminary crystallographic studies were performed. The crystal was grown at 277 K by the hanging-drop vapour-diffusion method. Native X-ray diffraction data were collected to 1.7 A resolution using synchrotron radiation at station BL38B1, SPring-8. The crystal belongs to space group P2(1), with unit-cell parameters a = 48.79, b = 84.06, c = 87.04 A. Assuming the presence of one molecule per asymmetric unit, the Matthews coefficient V(M) was calculated to be 2.73 A3 Da(-1) and the solvent content was 55%.
Angkawidjaja
Clement
C
Department of Material and Life Science, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan.
You
Dong-Ju
DJ
Matsumura
Hiroyoshi
H
Koga
Yuichi
Y
Takano
Kazufumi
K
Kanaya
Shigenori
S
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D045604:Extracellular Fluid / Q000201:enzymology*; D008049:Lipase / Q000096:biosynthesis* / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D005810:Multigene Family; D011549:Pseudomonas / Q000201:enzymology / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D008049:Lipase