title: Purification, crystallization and preliminary diffraction studies of an ectromelia virus glutaredoxin.
abstract: Ectromelia, vaccinia, smallpox and other closely related viruses of the orthopoxvirus genus encode a glutaredoxin gene that is not present in poxviruses outside of this genus. The vaccinia glutaredoxin O2L has been implicated as the reducing agent for ribonucleotide reductase and may thus play an important role in viral deoxyribonucleotide synthesis. As part of an effort to understand nucleotide metabolism by poxviruses, EVM053, the O2L ortholog of the ectromelia virus, has been crystallized. EVM053 crystallizes in space group C222(1), with unit-cell parameters a = 61.98, b = 67.57, c = 108.55 A. Diffraction data have been processed to 1.8 A resolution and a self-rotation function indicates that there are two molecules per asymmetric unit.
authors.affiliation: Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
authors.forename: John-Paul
authors.initials: JP
authors.lastname: Bacik
authors.forename: Angela M
authors.initials: AM
authors.lastname: Brigley
authors.forename: Lisa D
authors.initials: LD
authors.lastname: Channon
authors.forename: Gerald F
authors.initials: GF
authors.lastname: Audette
authors.forename: Bart
authors.initials: B
authors.lastname: Hazes
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D004481:Ectromelia virus / Q000737:chemistry*; D054477:Glutaredoxins; D009711:Nucleotides / Q000378:metabolism; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D054477:Glutaredoxins; D009711:Nucleotides; D014764:Viral Proteins; D010088:Oxidoreductases