Crystallization and preliminary X-ray crystallographic analysis of alginate lyase A1-II from Sphingomonas species A1.
Alginate lyase A1-II of Sphingomonas species A1 was purified and crystallized using the hanging drop vapor-diffusion method in 0.1 M Tris-HCl buffer containing 43% saturated ammonium sulfate, 8% polyethylene glycol 4000 and 0.2 M Li(2)SO(4) at pH 8.5 and 20 degrees C. The crystals are tetragonal and belong to the space group P4(3)2(1)2 or P4(1)2(1)2 with unit cell dimensions of a=b=144.07 and c=296.38 A. The diffraction data up to 2.8 A were collected by a synchrotron radiation source at SPring-8 in Japan.
Yoon
H J
HJ
Research Institute for Food Science, Kyoto University, Uji, Kyoto, Japan.
Hashimoto
W
W
Katsuya
Y
Y
Mezaki
Y
Y
Murata
K
K
Mikami
B
B
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D020578:Sphingomonas / Q000737:chemistry* / Q000201:enzymology
D001426:Bacterial Proteins; D011133:Polysaccharide-Lyases; C016158:poly(beta-D-mannuronate) lyase