Published May 24, 2013 | Version v1
Journal article

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

  • 1. Universidade de Fortaleza, Avenida Washington Soares 1321, Bairro Edson Queiroz, 60811-905 Fortaleza-CE (Brazil)
  • 2. Faculdade Estácio do Ceará Via Corpvs, Rua Eliseu Uchoa Becco 600, Bairro Água Fria, 60810-270 Fortaleza-CE (Brazil)
  • 3. Universidade Federal do Ceará, Campus do Pici, 60451-970 Fortaleza-CE (Brazil)

Description

An osmotin from the latex of C. procera has been crystallized in both tetragonal and trigonal forms suitable for structure determination. 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 P43) or using 0.1 M HEPES buffer pH 7.5, 35% MPD, 0.7 M ammonium sulfate (space group P3112). X-ray diffraction data were collected to 2.17 Å (P43) and 1.80 Å (P3112) resolution and molecular-replacement analyses produced initial phases for both crystal forms

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309113011378; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3668584

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
69
Journal Issue
Pt 6
Journal Page Range
p. 646-649
ISSN
1744-3091
CODEN
ACSFCL

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2013
Notes
PMCID: PMC3668584; PMID: 23722843; PUBLISHER-ID: en5534; OAI: oai:pubmedcentral.nih.gov:3668584