Preliminary X-ray crystallographic analysis of a plant defence protein, the polygalacturonase-inhibiting protein from Phaseolus vulgaris

A leucine-rich repeat plant protein involved in resistance to pathogens, a polygalacturonase-inhibiting protein (PGIP-1) from Phaseolus vulgaris, has been crystallized and preliminary X-ray characterization has been performed . The protein contains ten repeats of a short (24 amino-acid) leucine-rich repeat motif. Single crystals of the protein were grown from vapour-diffusi on experiments using PEG 2K monomethylether as precipitant; these crystals diffract to at least 2.3 Angstrom resolution. The space group is P2(1), wit h two molecules of PGIP-1 in the asymmetric unit; the crystals contain appr oximately 38% solvent.