Crystallization and preliminary X-ray study of isomaltodextranase from Arthrobacter globiformis.
A recombinant isomaltodextranase (1,6-alpha-D-glucan isomaltohydrolase; EC 3.2.1.94) from an Arthrobacter sp. that hydrolyzes dextrans to generate isomaltose was purified and crystallized using the sitting-drop vapour-diffusion method at 293 K. X-ray diffraction data were collected to 1.8 A. The crystals belong to space group C2, with unit-cell parameters a = 199.1, b = 62.7, c = 57.4, beta = 101.4 degrees. Analysis of the Patterson self-rotation function suggests that the crystal contains one protein molecule in the asymmetric unit.
Akita
Masatake
M
Japan Marine Science and Technology Center, 2-15 Natsushima, Yokosuka 237-0061, Japan. akitam@jamstec.go.jp
Mizuno
Masahiro
M
Tonozuka
Takashi
T
Sakano
Yoshiyuki
Y
Matsui
Hirokazu
H
Hidaka
Yuko
Y
Hatada
Yuji
Y
Ito
Susumu
S
Horikoshi
Koki
K
D001173:Arthrobacter / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003911:Dextrans / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000737:chemistry* / Q000378:metabolism; D007534:Isomaltose / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D003911:Dextrans; D011994:Recombinant Proteins; D007534:Isomaltose; D006026:Glycoside Hydrolases; C091051:glucan 1,6-alpha-isomaltosidase