Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase V.
Human peptidylarginine deiminase V (PAD V) is a post-translational enzyme that catalyzes the conversion of arginine residues in protein into citrulline residues in the presence of calcium ion. Crystals of PAD V have been grown at 293 K using polyethylene glycol monomethylether as a precipitant. Crystals diffracted beyond 2.7 A resolution at 100 K at the SPring-8 synchrotron-radiation source. The crystal belongs to space group C2, with unit-cell parameters a = 144.6, b = 60.4, c = 113.4 A, beta = 123.6 degrees. The asymmetric unit contains one molecule, with a V(M) of 2.56 A(3) Da(-1) and a solvent content of 56.1%. A full set of X-ray diffraction data was collected to 2.8 A resolution with a completeness of 97.5%. Heavy-atom derivatives have been successfully prepared and structure analysis is in progress.
Arita
Kyouhei
K
Graduate School of Integrated Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
Hashimoto
Hiroshi
H
Shimizu
Toshiyuki
T
Yamada
Michiyuki
M
Sato
Mamoru
M
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods / Q000706:statistics & numerical data; D004926:Escherichia coli / Q000378:metabolism; D006801:Humans; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics; D000080002:Protein-Arginine Deiminase Type 4; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D011994:Recombinant Proteins; D006867:Hydrolases; D000080002:Protein-Arginine Deiminase Type 4