Crystallization and oligomeric structure of rat liver arginase

• Published in: Journal of molecular biology Vol. 224; no. 4; pp. 1175 - 1177
• Main Authors: Kanyo, Zoltan F., Chen, Cheau-Yun, Daghigh, Farzaneh, Ash, David E., Christianson, David W.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 20.04.1992; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Animals; arginase; Arginase - ultrastructure; Biological and medical sciences; crystal structure; Crystallography; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; liver; Liver - enzymology; Macromolecular Substances; metalloenzyme; oligomers; protein structure; Rats; X-ray crystallography; X-Ray Diffraction; X-ray crystallography; protein structure; metalloenzyme; arginase; Vertebrata; Mammalia; Rat; Molecular structure; Enzyme; Liver; Rodentia; Crystallization; X ray spectrometry; Arginase; Metalloenzyme; Crystalline structure
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/0022-2836(92)90479-4

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 pyramidshaped. X-ray diffraction data are measured to a limiting resolution of 2·4 Å. 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.