Open AccessCrystallization and preliminary X‐ray crystallographic analysis of human peptidylarginine deiminase type I
Author(s) -
Unno Masaki,
Kinjo Saya,
Kizawa Kenji,
Takahara Hidenari
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113028704
Subject(s) - crystallization , polyethylene glycol , chemistry , crystallography , solvent , substrate (aquarium) , crystal (programming language) , biochemistry , organic chemistry , biology , ecology , computer science , programming language
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 P 6 1 , with unit‐cell parameters a = b = 90.3, c = 372.3 Å. The solvent content was 58.2%.