In:
Acta Crystallographica Section D Biological Crystallography, International Union of Crystallography (IUCr), Vol. 56, No. 1 ( 2000-01-01), p. 98-100
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 P 2 1 , with two molecules of PGIP-1 in the asymmetric unit; the crystals contain approximately 38% solvent.
Type of Medium:
Online Resource
ISSN:
0907-4449
DOI:
10.1107/S0907444999014316
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2000
detail.hit.zdb_id:
2968623-4
SSG:
12
SSG:
13
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