Crystallization and oligomeric structure of rat liver arginase

Document Type

Article

Publication Date

1992

Abstract

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.

Publication Title

Journal of Molecular Biology

Volume

224

Issue

4

First Page

1175

Last Page

1177

Comments

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.

This document is currently not available here.

COinS