Crystallization and X-ray crystallographic analysis of human STAT1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt 7):666-8. doi: 10.1107/S1744309105017392. Epub 2005 Jun 15.

Abstract

Unphosphorylated human STAT1 (1-683) has been crystallized in the presence of a phosphopeptide derived from the alpha-chain of human interferon gamma (IFNgamma) receptor. A complete data set has been collected from a KAu(CN)2-derivatized and dehydrated crystal. The crystal belonged to space group P6(1)22, with unit-cell parameters a = b = 102.6, c = 646.5 A, alpha = beta = 90, gamma = 120 degrees.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallography, X-Ray / methods*
  • Dimerization
  • Humans
  • Interferon-gamma / metabolism
  • Models, Statistical
  • Peptides / chemistry
  • Phosphorylation
  • Protein Conformation
  • Protein Structure, Tertiary
  • STAT1 Transcription Factor / chemistry*
  • X-Ray Diffraction

Substances

  • Peptides
  • STAT1 Transcription Factor
  • STAT1 protein, human
  • Interferon-gamma