Crystallization and preliminary crystallographic studies of the C-terminal domain of human FKBP52

Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2269-71. doi: 10.1107/s090744490301970x. Epub 2003 Nov 27.

Abstract

FKBP52 is a high-molecular-weight immunophilin belonging to the FKBP (FK506-binding protein) family. FKBP52 is one of several chaperone proteins associated with untransformed steroid receptors in steroid receptor-hsp90 heterocomplexes. Here, the C-terminal domain (amino acids 145-459) has been cloned, overexpressed and purified. Crystals were obtained using the hanging-drop vapour-diffusion technique with ammonium sulfate as precipitant in 0.1 M Tris pH 8.0 solution. Diffraction data to 2.7 A were collected from a selenomethionine-containing crystal belonging to space group C222(1), with unit-cell parameters a = 114.4, b = 143.1, c = 171.2 A, alpha = beta = gamma = 90 degrees. There are three molecules per asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization / methods
  • Crystallography, X-Ray / methods
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Humans
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Selenomethionine / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Tacrolimus Binding Proteins / chemistry*
  • Tacrolimus Binding Proteins / genetics

Substances

  • Recombinant Proteins
  • Selenomethionine
  • Tacrolimus Binding Proteins
  • tacrolimus binding protein 4