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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 6(69), p. 646-649, 2013

DOI: 10.1107/s1744309113011378

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

Journal article published in 2013 by Frederico Bruno-Moreno, Raquel Sombra Basílio de Oliveira, Renato de Azevedo Moreira ORCID, Marina Duarte Pinto Lobo, Marina Duarte Pinto Lobo, Cléverson Diniz Teixeira de Freitas, Marcio Viana Ramos, Márcio Viana Ramos, Thalles Barbosa Grangeiro, Thalles Barbosa Grangeiro, Ana Cristina Oliveira Monteiro-Moreira
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This paper is available in a repository.

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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 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.