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Expression, purification and crystallization of a lyssavirus matrix (M) protein.

DOI: 10.1107/S1744309108004557 DOI Help
PMID: 18391421 PMID Help

Authors: Rene Assenburg (Wellcome Trust Centre for Human Genetics, University of Oxford) , Olivier Delmas (UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur) , Stephen Graham (Wellcome Trust Centre for Human Genetics, University of Oxford) , Anil Verma (Wellcome Trust Centre for Human Genetics, University of Oxford) , Nick Berrow (Wellcome Trust Centre for Human Genetics, University of Oxford) , David I. Stuart (University of Oxford) , Raymond Owens (University of Oxford) , Hervé Bourhy (UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur) , Jonathan Grimes (Division of Structural Biology, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 64 , PAGES 258-262

State: Published (Approved)
Published: March 2008

Abstract: The matrix (M) proteins of lyssaviruses (family Rhabdoviridae) are crucial to viral morphogenesis as well as in modulating replication and transcription of the viral genome. To date, no high-resolution structural information has been obtained for full-length rhabdovirus M. Here, the cloning, expression and purification of the matrix proteins from three lyssaviruses, Lagos bat virus (LAG), Mokola virus and Thailand dog virus, are described. Crystals have been obtained for the full-length M protein from Lagos bat virus (LAG M). Successful crystallization depended on a number of factors, in particular the addition of an N-terminal SUMO fusion tag to increase protein solubility. Diffraction data have been recorded from crystals of native and selenomethionine-labelled LAG M to 2.75 and 3.0 Å resolution, respectively. Preliminary analysis indicates that these crystals belong to space group P6122 or P6522, with unit-cell parameters a = b = 56.9–57.2, c = 187.9–188.6 Å, consistent with the presence of one molecule per asymmetric unit, and structure determination is currently in progress.

Journal Keywords: matrix proteins; Rhabdoviridae; lyssaviruses; Lagos bat virus; SUMO tag

Subject Areas: Biology and Bio-materials

Facility: ESRF