Open AccessCrystallization and preliminary X‐ray analysis of isomaltase from Saccharomyces cerevisiae
Author(s) -
Yamamoto Keizo,
Miyake Hideo,
Kusunoki Masami,
Osaki Shigeyoshi
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910803114x
Subject(s) - isomaltose , crystallization , saccharomyces cerevisiae , hydrolysis , crystallography , chemistry , biochemistry , enzyme , maltose , yeast , organic chemistry
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 C 2, with unit‐cell parameters a = 95.67, b = 115.42, c = 61.77 Å, β = 91.17°. X‐ray diffraction data were collected to 1.35 Å resolution from a single crystal on a synchrotron‐radiation source.