Open AccessPreliminary crystallographic analysis of the Megavirus superoxide dismutase
Author(s) -
Lartigue Audrey,
Philippe Nadège,
Jeudy Sandra,
Abergel Chantal
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911204657x
Subject(s) - superoxide dismutase , escherichia coli , recombinant dna , capsid , biology , microbiology and biotechnology , dismutase , chemistry , oxidative stress , gene , biochemistry
Megavirus chilensis , a close relative of the Mimivirus giant virus, is able to replicate in Acanthamoeba castellanii . The first step of viral infection involves the internalization of the virions in host vacuoles. It has been experimentally demonstrated that Mimivirus particles contain many proteins capable of resisting oxidative stress, as encountered in the phagocytic process. These proteins are conserved in Megavirus , which has an additional gene (Mg277) encoding a putative superoxide dismutase. The Mg277 ORF product was overexpressed in Escherichia coli , purified and crystallized. A SAD data set was collected to 2.24 Å resolution at the selenium peak wavelength on the BM30 beamline at the ESRF from a single crystal of selenomethionine‐substituted recombinant superoxide dismutase protein.