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- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2011
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309110050785
- pmid
- 21206054
- Publisher site
- See Article on Publisher Site
Abstract
The complete genome sequence of the largest known double‐stranded DNA virus, mimivirus, reveals the presence of a gene (denoted R355) that potentially encodes a cysteine protease that is expressed late (after 6 h) in the infectious cycle of the virus. In order to verify a sequence‐based functional prediction and understand its role during the infectious process, the R355 protein was produced to assay its proteolytic activity and solve its three‐dimensional structure. Here, the preliminary crystallographic analysis of the recombinant viral protein is reported. The crystals belonged to the orthorhombic space group P212121, with a monomer in the asymmetric unit. A MAD data set was used for preliminary phasing using the selenium signal from a selenomethionine‐substituted protein crystal.
Journal
Acta Crystallographica Section F – Wiley
Published: Jan 1, 2011