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Crystallization and preliminary X‐ray diffraction analysis of a novel sphingomyelinase D from Loxosceles gaucho venom
Author(s) -
Ullah Anwar,
Magalhães Geraldo Santana,
Masood Rehana,
Mariutti Ricardo Barros,
Coronado Monika Aparecida,
Murakami Mário Tyago,
Barbaro Katia Cristina,
Arni Raghuvir Krishnaswamy
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14019207
Subject(s) - venom , crystallization , sphingomyelin , biology , materials science , chemistry , biochemistry , organic chemistry , membrane
Brown 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 P 2 1 2 1 2, with unit‐cell parameters a = 52.98, b = 62.27, c = 84.84 Å and diffracted to a maximum resolution of 2.6 Å.