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Higher plants contain several constitutively expressed proteins for protection
against infections by viruses, bacteria and fungi. Here we report the
crystallization of a polypeptide with antifungal activity, a 26,000 dalton
endochitinase from barley (Hordeum vulgare L.) seeds, in a form suitable for
high-resolution X-ray analysis. Crystals were grown by vapor diffusion under
several different conditions. The best crystals, obtained with ammonium sulfate
as the precipitant, belong to the tetragonal space group P4(1)2(1)2
(P4(3)2(1)2), with cell dimensions a = b = 62.9 A and c = 96.0 A. The cell
dimensions are consistent with one endochitinase molecule per asymmetric unit,
and the crystals diffract to at least 2.0 A resolution.
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