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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%.

SUBMITTER: Unno M

PROVIDER: S-EPMC3855719 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of human peptidylarginine deiminase type I.

Unno Masaki M Kinjo Saya S Kizawa Kenji K Takahara Hidenari H

Acta crystallographica. Section F, Structural biology and crystallization communications 20131128 Pt 12

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), ...[more]

PMID: 24316829

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