Crystallization of an endochitinase from Hordeum vulgare L. seeds

P. John Hart, Michael P. Ready, Jon D. Robertus

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

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 P412121 (P43212). 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 Å resolution.

Original languageEnglish (US)
Pages (from-to)565-567
Number of pages3
JournalJournal of Molecular Biology
Volume225
Issue number2
DOIs
StatePublished - May 20 1992

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Keywords

  • X-ray analysis
  • barley
  • crystallization
  • endochitinase

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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