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Crystallization of an apo form of human arginase: using all the tools in the toolbox simultaneously

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Arginase (EC 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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Keywords: alternative reservoirs; arginase; seeding

Document Type: Research Article

Publication date: January 1, 2011

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