Crystallization and preliminary X-ray diffraction analysis of a novel beta-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum
Zhu, Zhen1; He, Miao1; Huang, Chun-Hsiang2; Ko, Tzu-Ping3; Zeng, Yi-Fang4; Huang, Yu-Ning4; Jia, Shiru1; Lu, Fuping1; Liu, Je-Ruei4,5; Guo, Rey-Ting2
刊名ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
2014-05-01
卷号70页码:636-638
英文摘要The beta-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum JCM 1217 hydrolyzes the beta-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 P3(x)21, with unit-cell parameters a = b = 75.9, c = 254.0 angstrom, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.78 angstrom 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.
WOS标题词Science & Technology ; Life Sciences & Biomedicine ; Physical Sciences
类目[WOS]Biochemical Research Methods ; Biochemistry & Molecular Biology ; Biophysics ; Crystallography
研究领域[WOS]Biochemistry & Molecular Biology ; Biophysics ; Crystallography
关键词[WOS]EXTENSIN
收录类别SCI
语种英语
WOS记录号WOS:000335921500020
内容类型期刊论文
源URL[http://124.16.173.210/handle/834782/1358]  
专题天津工业生物技术研究所_结构生物学与蛋白酶学实验室 郭瑞庭_期刊论文
作者单位1.Tianjin Univ Sci & Technol, Coll Biotechnol, Tianjin Key Lab Ind Microbiol, Tianjin 300457, Peoples R China
2.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China
3.Acad Sinica, Inst Biol Chem, Taipei 115, Taiwan
4.Natl Taiwan Univ, Inst Biotechnol, Taipei 106, Taiwan
5.Natl Taiwan Univ, Dept Anim Sci & Technol, Taipei 106, Taiwan
推荐引用方式
GB/T 7714
Zhu, Zhen,He, Miao,Huang, Chun-Hsiang,et al. Crystallization and preliminary X-ray diffraction analysis of a novel beta-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum[J]. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS,2014,70:636-638.
APA Zhu, Zhen.,He, Miao.,Huang, Chun-Hsiang.,Ko, Tzu-Ping.,Zeng, Yi-Fang.,...&Guo, Rey-Ting.(2014).Crystallization and preliminary X-ray diffraction analysis of a novel beta-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum.ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS,70,636-638.
MLA Zhu, Zhen,et al."Crystallization and preliminary X-ray diffraction analysis of a novel beta-L-arabinofuranosidase (HypBA1) from Bifidobacterium longum".ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 70(2014):636-638.
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