title: Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously.
abstract: 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 P2(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.
authors.affiliation: Materials Science and Engineering, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia. janet.newman@csiro.au
authors.forename: Janet
authors.initials: J
authors.lastname: Newman
authors.forename: Lesley
authors.initials: L
authors.lastname: Pearce
authors.forename: Charles A
authors.initials: CA
authors.lastname: Lesburg
authors.forename: Corey
authors.initials: C
authors.lastname: Strickland
authors.forename: Thomas S
authors.initials: TS
authors.lastname: Peat
mesh_terms: D000818:Animals; D001119:Arginase / Q000037:antagonists & inhibitors / Q000737:chemistry*; D003460:Crystallization; D006801:Humans; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000737:chemistry*; D008969:Molecular Sequence Data
chemical_list: D007527:Isoenzymes; D001119:Arginase