Crystallization and preliminary X-ray crystallographic studies of α-galactosidase I from Mortierella vinacea

α‐Galactosidases catalyze the hydrolysis of a galactosyl residue from galactooligosaccharides and galactopolysaccharides. α‐Galactosidase I from Mortierella vinacea was crystallized in two crystal forms using the hanging‐drop vapour‐diffusion method. Type 1 crystals belonged to space group I422, wit...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-12, Vol.59 (12), p.2289-2291
Main Authors: Fujimoto, Zui, Kim, Wook-Dong, Kaneko, Satoshi, Park, Gwi-Gun, Momma, Mitsuru, Kobayashi, Hideyuki, Mizuno, Hiroshi
Format: Article
Language:English
Subjects:
alpha-Galactosidase - chemistry
Bacterial Proteins - chemistry
Crystallization - methods
Crystallography, X-Ray
Fungal Proteins - chemistry
glycoprotein
glycosyl hydrolase family 27
Mortierella - enzymology
Mortierella vinacea
Protein Structure, Quaternary
α-galactosidase
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Summary:α‐Galactosidases catalyze the hydrolysis of a galactosyl residue from galactooligosaccharides and galactopolysaccharides. α‐Galactosidase I from Mortierella vinacea was crystallized in two crystal forms using the hanging‐drop vapour‐diffusion method. Type 1 crystals belonged to space group I422, with unit‐cell parameters a = b = 142.4, c = 131.5 Å, and diffracted to beyond 2.1 Å resolution, while type 2 crystals belonged to space group P4, with unit‐cell parameters a = b = 100.9, c = 102.7 Å, and diffracted to beyond 1.6 Å resolution. This enzyme crystallized as a glycoprotein tetramer and the tetrameric structure was located around the crystallographic fourfold axis.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444903019681