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Acta Crystallogr D Biol Crystallogr. 1994 Mar 01;50:175-7. doi: 10.1107/S0907444993009989.

Crystallization of biosynthetic arginine decarboxylase from Escherichia coli.

Acta crystallographica. Section D, Biological crystallography

B R Rodrigez, D W Carroll, D Mitchell, C Momany, M L Hackert

Affiliations

  1. Department of Chemistry and Biochemistry, University of Texas at Austin, 78712, USA.

PMID: 15299455 DOI: 10.1107/S0907444993009989

Abstract

Putrescine is the immediate precursor for the synthesis of polyamines and is normally generated by the action of ornithine decarboxylase. However, putrescine can also be produced by the conversion of arginine to agmatine by arginine decarboxylase (bADC) followed by the release of urea by agmatine ureohydrolase. Amino-acid sequence homology with the eukaryotic ornithine decarboxylases suggests that bADC may be a model for this group of decarboxylases. We report here the crystallization of arginine decarboxylase from E. coli. Crystals up to 1 mm in size are grown by vapor equilibration using Li(2)SO(4) and polyethylene glycols as precipitants. The crystals exhibit diffraction maxima beyond 3 A resolution and belong to space group P4(1(3))2(1)2 with a = 192.4 and c = 121.0 A. These unit-cell dimensions together with the estimated density of the crystals suggest the presence of one tetramer of bADC (71 kDa subunit(-1)) per asymmetric unit (V(m) = 2.0 A(3) Da(-1)).

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