Crystallization and preliminary X-ray study of biosynthetic alanine racemase from Pseudomonas aeruginosa PAO1

被引：1

作者：

Zhou, Honggang ^{[1
]}

Li, Zhenzhen ^{[2
]}

Zhang, Guofang ^{[2
]}

Xu, Shujing ^{[3
]}

Tang, Zhaona ^{[2
]}

Zhu, Xianming ^{[2
]}

Dong, Hui ^{[2
,4
,5
]}

Ju, Jiansong ^{[3
]}

机构：

[1] Nankai Univ, Coll Pharm, State Key Lab Med Chem Biol, Tianjin 300071, Peoples R China

[2] Tianjin Int Joint Acad Biomed, Tianjin 300457, Peoples R China

[3] Hebei Normal Univ, Coll Life Sci, Shijiazhuang 050024, Peoples R China

[4] Chinese Acad Med Sci, Key Lab Tianjin Radiat & Mol Nucl Med, Inst Radiat Med, Tianjin 300192, Peoples R China

[5] Peking Union Med Coll, Tianjin 300192, Peoples R China

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2014年 / 70卷

基金：

中国国家自然科学基金;

关键词：

ESCHERICHIA-COLI; CRYSTALS;

D O I：

10.1107/S2053230X14022432

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Biosynthetic alanine racemase (Alr(PA)) from Pseudomonas aeruginosa PAO1 carrying a His(6) tag was expressed in Escherichia coli BL21 (DE3) cells and purified by Ni2+-chelating affinity and anion-exchange chromatography for X-ray crystallographic analysis. Crystals were grown by the hanging-drop vapour-diffusion method at 289 K in a solution consisting of 4%(v/v) Tacsimate pH 5.0, 14%(w/v) polyethylene glycol 3350 with a protein concentration of 8 mg ml(-1). The crystal diffracted to 2.76 angstrom resolution and belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 74.12, b = 76.97, c = 154.80 angstrom, alpha = beta = gamma = 90 degrees.

引用

页码：1616 / 1619

页数：4

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