Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously
Arginase (EC 188.8.131.52) 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 P212121 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.
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