title: Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type I.
abstract: Peptidylarginine deiminase (PAD) catalyzes the post-translational conversion of peptidylarginine to peptidylcitrulline in the presence of calcium ions. Among the five known human PAD isozymes (PAD1-4 and PAD6), PAD1 exhibits the broadest substrate specificity. Crystals of PAD1 obtained using polyethylene glycol 3350 as a precipitant diffracted to 3.70 Å resolution using synchrotron radiation. Two PAD1 molecules were contained in the asymmetric unit and the crystals belonged to space group P6(1), with unit-cell parameters a = b = 90.3, c = 372.3 Å. The solvent content was 58.2%.
authors: Frontier Research Center for Applied Atomic Sciences, Ibaraki University, 162-1 Shirakata, Tokai, Naka, Ibaraki 319-1106, Japan.
authors: Masaki
authors: M
authors: Unno
authors: Saya
authors: S
authors: Kinjo
authors: Kenji
authors: K
authors: Kizawa
authors: Hidenari
authors: H
authors: Takahara
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics; D011092:Polyethylene Glycols / Q000737:chemistry; D055503:Protein Multimerization; D000080062:Protein-Arginine Deiminase Type 1; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017356:Synchrotrons
chemical_list: D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D006867:Hydrolases; D000080062:Protein-Arginine Deiminase Type 1
keywords: isozymes; peptidylarginine deiminase; post-translational modification; substrate specificity