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 P31 (or P32) with hexagonal unit cell dimensions a = b = 88·9 Å, c = 114·8 Å, or a = b = 88·5 Å, c = 104·5 Å; 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.
Journal of Molecular Biology
Kanyo, Zoltan F.; Chen, Cheau-Yun; Daghigh, Farzaneh; Ash, David E.; and Christianson, David W., "Crystallization and oligomeric structure of rat liver arginase" (1992). PCOM Scholarly Papers. 1036.
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