Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa L-arginine deiminase.
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.
Oudjama
Yamina
Y
Institut de Recherches Microbiologiques JM Wiame, 1 Avenue E Gryzon, 1070 Bruxelles, Belgium.
Tricot
Catherine
C
Stalon
Victor
V
Wouters
Johan
J
D001483:Base Sequence; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011487:Protein Conformation; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification
D017931:DNA Primers; D011994:Recombinant Proteins; D006867:Hydrolases; C019723:arginine deiminase