Crystallization and oligomeric structure of rat liver arginase.
Rat liver arginase, a manganese-metalloenzyme, has been crystallized from polyethylene glycol 8000 in N,N-bis(2-hydroxyethyl)glycine (Bicine) buffer at pH 8.5. Crystals form as either cubes or pyramids and belong to space group P3(1) (or P3(2)) with hexagonal unit cell dimensions a = b = 88.9 A, c = 114.8 A, or a = b = 88.5 A, c = 104.5 A; the variation along the c axis does not correlate with the external crystal morphology of cube or pyramid-shaped. X-ray diffraction data are measured to a limiting resolution of 2.4 A. Given the volume constraints of the unit cell it is likely that rat liver arginase is a trimer, with three 35,000 Da monomers in the asymmetric unit. This resolves a persistent ambiguity regarding the oligomeric structure of this enzyme.
Kanyo
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Department of Chemistry, University of Pennsylvania, Philadelphia 19104-6323.
Chen
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Daghigh
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Ash
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Christianson
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D000818:Animals; D001119:Arginase / Q000648:ultrastructure*; D003461:Crystallography; D008099:Liver / Q000201:enzymology; D046911:Macromolecular Substances; D051381:Rats; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D001119:Arginase