Expression, purification, crystallization and initial X-ray diffraction analysis of thiol peroxidase from Yersinia pseudotuberculosis.
Thiol peroxidase is an atypical 2-Cys peroxiredoxin that reduces alkyl hydroperoxides. Wild-type and C61S mutant protein have been recombinantly expressed in Escherichia coli and purified using nickel-affinity chromatography. Initial crystallization trials yielded three crystal forms in three different space groups (P2(1), P6(4) and P2(1)2(1)2(1)) both in the presence and the absence of DTT.
Institute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, Glasgow Biomedical Research Centre, Glasgow G12 8QQ, Scotland. mads.gabrielsen@glasgow.ac.uk
Mads
M
Gabrielsen
Caroline E
CE
Zetterström
Dai
D
Wang
Katherine S H
KS
Beckham
Mikael
M
Elofsson
Neil W
NW
Isaacs
Andrew J
AJ
Roe
D003460:Crystallization; D018360:Crystallography, X-Ray; D010544:Peroxidases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D014961:X-Ray Diffraction; D015011:Yersinia pseudotuberculosis / Q000201:enzymology*
D010544:Peroxidases; C058652:thiol-dependent peroxidase