Crystallization of a stringent response factor from Aquifex aeolicus.

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Abstract

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.

Detaljer

Författare
  • Ole Kristensen
  • Martin Laurberg
  • Michael Gajhede
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Strukturbiologi
Originalspråkengelska
Sidor (från-till)1198-1200
TidskriftActa Crystallographica. Section D: Biological Crystallography
Volym58
Utgåva nummerPt 7
StatusPublished - 2002
PublikationskategoriForskning
Peer review utfördJa