Literature DB >> 12499553

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

Nan Li1, Daohai Zhang, Lian-Hui Zhang, Kunchithapadam Swaminathan.   

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.

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Year:  2002        PMID: 12499553     DOI: 10.1107/s0907444902017547

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Expression, purification, crystallization and preliminary X-ray crystallographic studies of the trehalulose synthase MutB from Pseudomonas mesoacidophila MX-45.

Authors:  Stéphanie Ravaud; Hildegard Watzlawick; Richard Haser; Ralf Mattes; Nushin Aghajari
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2004-12-02
  1 in total

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