Crystallization of a stringent response factor from Aquifex aeolicus.
The crystallization of a key enzyme from Aquifex aeolicus with suggested bifunctional activity, acting as an exopolyphosphatase and a guanosine pentaphosphate phosphohydrolase, is reported. Native data were collected to below 2 A resolution from an orthorhombic crystal with unit-cell parameters a = 50.8, b = 70.3, c = 90.9 A. Methionine residues were introduced by mutation and deliberate oxidation of the protein allowed us to produce additional crystal forms with reproducible diffraction ability and increased phasing potential. This is the first report on the crystallization of a member of the Ppx/GppA phosphatase family.
Kristensen
Ole
O
Protein Structure Group, Department of Chemistry, University of Copenhagen, Universitetsparken 5, Denmark. olek@psg.ki.ku.dk
Laurberg
Martin
M
Gajhede
Michael
M
D001419:Bacteria / Q000201:enzymology*; D002850:Chromatography, Gel; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray / Q000379:methods*; D019281:Dimerization; D004220:Disulfides; D004591:Electrophoresis, Polyacrylamide Gel; D006861:Hydrogen Peroxide / Q000737:chemistry; D009154:Mutation; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000302:isolation & purification*; D016133:Polymerase Chain Reaction; D012984:Software
D004220:Disulfides; D006861:Hydrogen Peroxide; D010749:Phosphoprotein Phosphatases; C080406:protein phosphatase 4