Crystallization and preliminary X‐ray study of biosynthetic alanine racemase from Pseudomonas aeruginosa PAO1. Issue 12 (1st December 2014)

• Record Type: Journal Article
• Authors: Zhou, Honggang; Li, Zhenzhen; Zhang, Guofang; Xu, Shujing; Tang, Zhaona; Zhu, Xianming; Dong, Hui; Ju, Jiansong
• Is Part Of: Acta crystallographica. Volume 70:Issue 12(2014:Dec.)
• Page Start: 1616
• Page End: 1619
• Publication Date: 2014-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14022432
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Biosynthetic alanine racemase (Alr_PA) from <italic>Pseudomonas aeruginosa</italic> PAO1 carrying a His₆ tag was expressed in <italic>Escherichia coli</italic> 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%(<italic>v</italic>/<italic>v</italic>) Tacsimate pH 5.0, 14%(<italic>w</italic>/<italic>v</italic>) 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 <italic>P</italic>2₁2₁2₁, with unit‐cell parameters <italic>a</italic> = 74.12, <italic>b</italic> = 76.97, <italic>c</italic> = 154.80 Å, α = β = γ = 90°.</p> </abstract>