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

ABSTRACT: Biosynthetic alanine racemase (AlrPA) from Pseudomonas aeruginosa PAO1 carrying a His6 tag was expressed in Escherichia coli BL21 (DE3) cells and purified by Ni(2+)-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?Å resolution and belonged to the orthorhombic space group P212121, with unit-cell parameters a = 74.12, b = 76.97, c = 154.80?Å, ? = ? = ? = 90°.

SUBMITTER: Zhou H

PROVIDER: S-EPMC4259224 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature

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

Zhou Honggang H Li Zhenzhen Z Zhang Guofang G Xu Shujing S Tang Zhaona Z Zhu Xianming X Dong Hui H Ju Jiansong J

Acta crystallographica. Section F, Structural biology communications 20141114 Pt 12

Biosynthetic alanine racemase (AlrPA) from Pseudomonas aeruginosa PAO1 carrying a His6 tag was expressed in Escherichia coli BL21 (DE3) cells and purified by Ni(2+)-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 Å resolu ...[more]

PMID: 25484210

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