Open AccessCrystallization and preliminary X‐ray crystallographic analysis of human phosphodiesterase 12
Author(s) -
Kohno Tetsuya,
Yamaguchi Hiroto,
Hakoshima Toshio
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110008766
Subject(s) - crystallization , endonuclease , phosphodiesterase , exonuclease , crystallography , cloning (programming) , dna , homology (biology) , molecule , hydrolysis , chemistry , phosphatase , stereochemistry , enzyme , biochemistry , dna polymerase , organic chemistry , gene , computer science , programming language
Phosphodiesterase PDE12 is a medically important esterase‐family member that hydrolyzes 2′–5′‐linked oligoadenylates (2‐5A), which are involved in the regulation of biological processes related to the antiviral and antitumour activity that can be induced by interferons. Here, cloning, purification and crystallization of the C‐terminal endonuclease/exonuclease/phosphatase‐homology domain of human PDE12 is reported. The crystals belonged to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 111.3, c = 192.4 Å, and diffracted to 2.5 Å resolution. Assuming the presence of three molecules in the asymmetric unit, the solvent content was estimated to be about 44.0%.