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Crystallization and preliminary X‐ray diffraction analysis of a novel β‐L‐arabinofuranosidase (HypBA1) from Bifidobacterium longum
Author(s) -
Zhu Zhen,
He Miao,
Huang ChunHsiang,
Ko TzuPing,
Zeng YiFang,
Huang YuNing,
Jia Shiru,
Lu Fuping,
Liu JeRuei,
Guo ReyTing
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14001812
Subject(s) - bifidobacterium longum , recombinant dna , crystallography , chemistry , escherichia coli , glycoside hydrolase , crystallization , lactose , microbiology and biotechnology , biology , enzyme , biochemistry , bifidobacterium , gene , organic chemistry , fermentation , lactobacillus
The β-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum JCM 1217 hydrolyzes the β-1,2-linked arabinofuranose disaccharide to release L-arabinoses. HypBA1 was classified into glycoside hydrolase family 127 (GH127) by the CAZy website (http://www.cazy.org/). The enzyme was expressed in Escherichia coli and the purified recombinant protein was crystallized. Crystals belonging to the primitive hexagonal space group P3x21, with unit-cell parameters a = b = 75.9, c = 254.0Å, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.78Å resolution. A BLASTP search (http://blast.ncbi.nlm.nih.gov/) of the Protein Data Bank did not reveal any similar crystal structures. Structural determination by using SeMet MAD and MIR methods is in progress.