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 3.70Å resolution using synchrotron radiation. Two PAD1 molecules were contained in the asymmetric unit and the crystals belonged to space group P61, with unit-cell parameters a = b = 90.3, c = 372.3Å. The solvent content was 58.2%. © 2013 International Union of Crystallography.