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Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae.

ABSTRACT: 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.

SUBMITTER: Yamamoto K

PROVIDER: S-EPMC2581680 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae.

Yamamoto Keizo K Miyake Hideo H Kusunoki Masami M Osaki Shigeyoshi S

Acta crystallographica. Section F, Structural biology and crystallization communications 20081028 Pt 11

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 ...[more]

PMID: 18997332

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