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

Autor: Bruno-Moreno F; Centro de Ciências da Saúde, Universidade de Fortaleza, Avenida Washington Soares 1321, Bairro Edson Queiroz, 60811-905 Fortaleza-CE, Brazil., Sombra Basílio de Oliveira R, de Azevedo Moreira R, Pinto Lobo MD, Teixeira de Freitas CD, Viana Ramos M, Barbosa Grangeiro T, Oliveira Monteiro-Moreira AC
Jazyk: angličtina
Zdroj: Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2013 Jun; Vol. 69 (Pt 6), pp. 646-9. Date of Electronic Publication: 2013 May 24.
DOI: 10.1107/S1744309113011378
Abstrakt: 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.
Databáze: MEDLINE