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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):1024-6. doi: 10.1107/S174430910803114X. Epub 2008 Oct 28.

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

Author information

1
Faculty of Medicine, Nara Medical University, Japan. kama@naramed-u.ac.jp

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.

PMID:
18997332
PMCID:
PMC2581680
DOI:
10.1107/S174430910803114X
[Indexed for MEDLINE]
Free PMC Article

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