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- W2017298905 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." @default.
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- W2017298905 date "2002-11-26" @default.
- W2017298905 modified "2023-09-27" @default.
- W2017298905 title "Overexpression, purification, crystallization and preliminary X-ray crystallographic analysis of<i>Pseudomonas aeruginosa</i><scp>L</scp>-arginine deiminase" @default.
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- W2017298905 doi "https://doi.org/10.1107/s0907444902015743" @default.
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