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Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa L-arginine deiminase.

作者信息

Oudjama Yamina, Tricot Catherine, Stalon Victor, Wouters Johan

机构信息

Institut de Recherches Microbiologiques JM Wiame, 1 Avenue E Gryzon, 1070 Bruxelles, Belgium.

出版信息

Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2150-2. doi: 10.1107/s0907444902015743. Epub 2002 Nov 23.

DOI:10.1107/s0907444902015743
PMID:12454483
Abstract

Pseudomonas aeruginosa L-arginine deiminase, an enzyme catalyzing the irreversible catabolism of arginine to citrulline, has been produced in selenomethionyl form. The protein was purified and crystallized by the sitting-drop vapour-diffusion method using a precipitant solution consisting of 55% MPD, 100 mM cacodylate pH 6.5, 20 mM MgCl(2). Crystals display tetragonal symmetry (P4(1)2(1)2 or P4(3)2(1)2), with unit-cell parameters a = b = 106.0, c = 300.2 A, and diffract to 2.7 A resolution. A complete MAD data set was collected to 3.2 A resolution on beamline BM30 at ESRF.

摘要

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