Crystallization and preliminary X-ray diffraction analysis of a novel sphingomyelinase D from Loxosceles gaucho venom

Ullah, Anwar [UNESP]Magalhaes, Geraldo SantanaMasood, Rehana [UNESP]Mariutti, Ricardo Barros [UNESP]Coronado, Monika Aparecida [UNESP]Murakami, Mario TyagoBarbaro, Katia CristinaArni, Raghuvir Krishnaswamy [UNESP]2015-03-182015-03-182014-10-01Acta Crystallographica Section F-structural Biology Communications. Hoboken: Wiley-blackwell, v. 70, p. 1418-1420, 2014.1744-3091http://hdl.handle.net/11449/117063Brown spider envenomation results in dermonecrosis, intravascular coagulation, haemolysis and renal failure, mainly owing to the action of sphingomyelinases D (SMases D), which catalyze the hydrolysis of sphingomyelin to produce ceramide 1-phosphate and choline or the hydrolysis of lysophosphatidylcholine to produce lysophosphatidic acid. Here, the heterologous expression, purification, crystallization and preliminary X-ray diffraction analysis of LgRec1, a novel SMase D from Loxosceles gaucho venom, are reported. The crystals belonged to space group P2(1)2(1)2, with unit-cell parameters a = 52.98, b = 62.27, c = 84.84 angstrom and diffracted to a maximum resolution of 2.6 angstrom.1418-1420engCrystallization and preliminary X-ray diffraction analysis of a novel sphingomyelinase D from Loxosceles gaucho venomArtigo10.1107/S2053230X14019207WOS:000343060200024Acesso restrito91625089789458870000-0003-2460-1145