Crystallization of a stringent response factor from Aquifex aeolicus

Research output: Contribution to journalJournal articlepeer-review

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.
Original languageEnglish
JournalActa Crystallographica. Section D: Biological Crystallography
Issue numberPt 7
Pages (from-to)1198-200
Number of pages3
Publication statusPublished - 2002

    Research areas

  • Bacteria, Chromatography, Gel, Cloning, Molecular, Crystallography, X-Ray, Dimerization, Disulfides, Electrophoresis, Polyacrylamide Gel, Hydrogen Peroxide, Mutation, Phosphoprotein Phosphatases, Polymerase Chain Reaction, Software

ID: 40318741