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Expression, crystallization and preliminary X-ray analysis of isomaltulose synthase (PalI) from Klebsiella sp. LX3

Authors :
Nan Li
Lian-Hui Zhang
Daohai Zhang
Kunchithapadam Swaminathan
Source :
Acta crystallographica. Section D, Biological crystallography. 59(Pt 1)
Publication Year :
2002

Abstract

Isomaltulose synthase (PalI) catalyzes the hydrolysis of the alpha-1,2 bond between the glucose and fructose moieties of sucrose and the formation of alpha-1,6 and alpha-1,1 bonds between the two components to produce isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofranose) and trehalulose (alpha-D-glucosylpyranosyl-1,1-D-fructofranose), respectively. The PalI protein has been overexpressed, purified and crystallized at 295 K using the hanging-drop vapour-diffusion method. The crystals diffract to 2.2 A resolution using synchrotron radiation and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 59.239, b = 94.153, c = 111.294 A.

Details

ISSN :
09074449
Volume :
59
Issue :
Pt 1
Database :
OpenAIRE
Journal :
Acta crystallographica. Section D, Biological crystallography
Accession number :
edsair.doi.dedup.....5208e8b2025c910a0b73f40f1ad2e803