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.
This article was published in Journal of Molecular Biology, Volume 224, Issue 4, Pages 1175-1177.The published version is available at http://dx.doi.org/10.1016/0022-2836(92)90479-4.
Copyright © 1992 Elsevier.