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

Leech, Andrew, Mattei, Benedetta, Federici, Luca, De Lorenzo, Giuli and Hemmings, Andrew M. (2000) Preliminary X-ray crystallographic analysis of a plant defence protein, the polygalacturonase-inhibiting protein from Phaseolus vulgaris. Acta Crystallographica Section D: Biological Crystallography, 56 (1). pp. 98-100. ISSN 0907-4449

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Abstract

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-diffusion experiments using PEG 2K monomethylether as precipitant; these crystals diffract to at least 2.3 Å resolution. The space group is P21, with two molecules of PGIP-1 in the asymmetric unit; the crystals contain approximately 38% solvent.

Item Type:	Article
Uncontrolled Keywords:	structural biology ,/dk/atira/pure/subjectarea/asjc/1300/1315
Faculty \ School:	Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	13 Feb 2025 17:30
Last Modified:	16 Feb 2025 06:30
URI:	https://ueaeprints.uea.ac.uk/id/eprint/98479
DOI:	10.1107/S0907444999014316

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