1. Preliminary crystallographic analysis of a polyadenylate synthase fromMegavirus
- Author
-
Sandra Jeudy, Chantal Abergel, Audrey Lartigue, and Lionel Bertaux
- Subjects
Polyadenylation ,Protein Conformation ,Molecular Sequence Data ,Biophysics ,Crystallography, X-Ray ,Biochemistry ,Genome ,Viral Proteins ,Structural Biology ,Genetics ,Polyadenylate ,Megaviridae ,Giant Virus ,Mimiviridae ,Mimivirus ,Base Sequence ,biology ,Polynucleotide Adenylyltransferase ,Condensed Matter Physics ,biology.organism_classification ,Crystallography ,Crystallization Communications ,Megavirus ,Crystallization - Abstract
Megavirus chilensis, a close relative of the Mimivirus giant virus, is also the most complex virus sequenced to date, with a 1.26 Mb double-stranded DNA genome encoding 1120 genes. The two viruses share common regulatory elements such as a peculiar palindrome governing the termination/polyadenylation of viral transcripts. They also share a predicted polyadenylate synthase that presents a higher than average percentage of residue conservation. The Megavirus enzyme Mg561 was overexpressed in Escherichia coli, purified and crystallized. A 2.24 Å resolution MAD data set was recorded from a single crystal on the ID29 beamline at the ESRF.
- Published
- 2012