Open AccessCrystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously
Author(s) -
Newman Janet,
Pearce Lesley,
Lesburg Charles A.,
Strickland Corey,
Peat Thomas S.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110046208
Subject(s) - toolbox , crystallization , arginase , materials science , chemistry , computer science , biochemistry , programming language , arginine , organic chemistry , amino acid
Arginase (EC 3.5.3.1) is an aminohydrolase that acts on l ‐arginine to produce urea and ornithine. Two isotypes of the enzyme are found in humans. Type I is predominantly produced in the liver and is a homotrimer of 35 kDa subunits. Human arginase (hArginase) I is seen to be up‐regulated in many diseases and is a potential therapeutic target for many diverse indications. Previous reports of crystallization and structure determination of hArginase have always included inhibitors of the enzyme: here, the first case of a true apo crystal form of the enzyme which is suitable for small‐molecule soaking is reported. The crystals belonged to space group P 2 1 2 1 2 1 and have approximate unit‐cell parameters a = 53, b = 67.5, c = 250 Å. The crystals showed slightly anisotropic diffraction to beyond 2.0 Å resolution.