Purification, crystallization and preliminary diffraction studies of an ectromelia virus glutaredoxin.
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.
Bacik
John-Paul
JP
Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Brigley
Angela M
AM
Channon
Lisa D
LD
Audette
Gerald F
GF
Hazes
Bart
B
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
D054477:Glutaredoxins; D009711:Nucleotides; D014764:Viral Proteins; D010088:Oxidoreductases