TY - JOUR
T1 - Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of Pseudomonas aeruginosa L-arginine deiminase
AU - Oudjama, Yamina
AU - Tricot, Catherine
AU - Stalon, Victor
AU - Wouters, Johan
PY - 2002/12/1
Y1 - 2002/12/1
N2 - 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 MgCl2. Crystals display tetragonal symmetry (P41212 or P43212), with unit-cell parameters a = b = 106.0, c = 300.2 Å, and diffract to 2.7 Å. resolution. A complete MAD data set was collected to 3.2 Å resolution on beamline BM30 at ESRF.
AB - 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 MgCl2. Crystals display tetragonal symmetry (P41212 or P43212), with unit-cell parameters a = b = 106.0, c = 300.2 Å, and diffract to 2.7 Å. resolution. A complete MAD data set was collected to 3.2 Å resolution on beamline BM30 at ESRF.
UR - http://www.scopus.com/inward/record.url?scp=0036898591&partnerID=8YFLogxK
U2 - 10.1107/S0907444902015743
DO - 10.1107/S0907444902015743
M3 - Article
C2 - 12454483
AN - SCOPUS:0036898591
SN - 0907-4449
VL - 58
SP - 2150
EP - 2152
JO - Acta crystallographica. Section D: Biological crystallography
JF - Acta crystallographica. Section D: Biological crystallography
IS - 12
ER -