Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae.
Isomaltase from Saccharomyces cerevisiae is an oligo-1,6-glucosidase that preferentially hydrolyzes isomaltose, with little activity towards isomaltotriose or longer oligosaccharides. An amino-acid sequence analysis of the isomaltase revealed that it belongs to glucoside hydrolase family 13. Recombinant isomaltase was purified and crystallized by the hanging-drop vapour-diffusion method with PEG 3350 as the precipitant. The crystals belonged to space group C2, with unit-cell parameters a = 95.67, b = 115.42, c = 61.77 A, beta = 91.17 degrees . X-ray diffraction data were collected to 1.35 A resolution from a single crystal on a synchrotron-radiation source.
Yamamoto
Keizo
K
Faculty of Medicine, Nara Medical University, Japan. kama@naramed-u.ac.jp
Miyake
Hideo
H
Kusunoki
Masami
M
Osaki
Shigeyoshi
S
D003460:Crystallization; D009834:Oligo-1,6-Glucosidase / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D009834:Oligo-1,6-Glucosidase