Expression, purification, crystallization and preliminary X-ray analysis of alpha-L-arabinofuranosidase B from Aspergillus kawachii.

نویسندگان

  • Akimasa Miyanaga
  • Takuya Koseki
  • Hiroshi Matsuzawa
  • Takayoshi Wakagi
  • Hirofumi Shoun
  • Shinya Fushinobu
چکیده

Alpha-L-Arabinofuranosidase (EC 3.2.1.55) is one of the hemicellulases that cleave the glycosidic bonds between L-arabinofuranoside side chains and various oligosaccharides. In this study, the first crystallization and preliminary X-ray analysis of alpha-L-arabinofuranosidase B from Aspergillus kawachii IFO4308 (AkAbfB), a family 54 glycoside hydrolase, is described. Recombinant AkAbfB was expressed in Escherichia coli and Pichia pastoris. The native crystals of recombinant AkAbfB produced by P. pastoris belong to the orthorhombic space group P2(1)2(1)2(1) (unit-cell parameters a = 39.5, b = 98.2, c = 144.0 A) and diffracted X-rays to a resolution of 1.82 A.

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عنوان ژورنال:
  • Acta crystallographica. Section D, Biological crystallography

دوره 60 Pt 7  شماره 

صفحات  -

تاریخ انتشار 2004