Crystallization and X-ray diffraction analysis of an antifungal laticifer protein

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):646-9. doi: 10.1107/S1744309113011378. Epub 2013 May 24.

Abstract

An osmotin (CpOsm) from the latex of Calotropis procera has been crystallized in both tetragonal and trigonal forms suitable for structure determination. Crystallographic studies of CpOsm are of great interest because limited information is available concerning the structure of latex proteins and CpOsm has previously been shown to interact with the spore membranes of some plant pathogenic fungi, thus impairing spore germination and hyphal growth. CpOsm crystals were grown using 0.1 M HEPES buffer pH 7.5, 26% PEG 4000, 0.2 M ammonium sulfate (space group P4(3)) or using 0.1 M HEPES buffer pH 7.5, 35% MPD, 0.7 M ammonium sulfate (space group P3(1)12). X-ray diffraction data were collected to 2.17 Å (P4(3)) and 1.80 Å (P3(1)12) resolution and molecular-replacement analyses produced initial phases for both crystal forms.

Keywords: Calotropis procera; PR-5; latex proteins; osmotins; thaumatin-like proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antifungal Agents / chemistry*
  • Antifungal Agents / isolation & purification
  • Calotropis*
  • Crystallization
  • Latex / chemistry*
  • Latex / isolation & purification
  • Plant Extracts / chemistry
  • Plant Extracts / isolation & purification
  • Plant Proteins / chemistry*
  • Plant Proteins / isolation & purification
  • Spectrometry, Mass, Electrospray Ionization
  • X-Ray Diffraction

Substances

  • Antifungal Agents
  • Latex
  • Plant Extracts
  • Plant Proteins