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Updated: May 16, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Preliminary crystallographic analysis of the Megavirus superoxide dismutase
Audrey Lartigue1, Nadège Philippe, Sandra Jeudy
1Information Génomique et Structurale, IGS UMR7256, CNRS, Aix-Marseille Université, IMM, FR3479, 163 Avenue de Luminy-case 934, 13288 Marseille CEDEX 09, France.
Abstract:
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.

