Crystallization and preliminary X-ray crystallographic studies of cPOP1

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):292-4. doi: 10.1107/S1744309113002686. Epub 2013 Feb 23.

Abstract

Cellular pyrin domain-only protein 1 (cPOP1) is a pyrin domain (PYD)-containing protein that can regulate inflammation by preventing the assembly of inflammasome via direct interaction with ASC (apoptosis-associated speck-like protein containing a caspase recruitment domain). In this study, cPOP1, corresponding to amino acids 1-87, was overexpressed in Escherichia coli using an engineered C-terminal polyhistidine tag. cPOP1 was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 3.6 Å from a crystal belonging to the cubic space group P2₁3 with unit-cell parameters a=b=c=94.12 Å, α=β=γ=90.00°.

Keywords: cPOP1; inflammasome; inflammation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Cytoskeletal Proteins / chemistry*
  • Cytoskeletal Proteins / genetics
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Histidine / genetics
  • Humans
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics
  • Protein Structure, Tertiary
  • Pyrin
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics

Substances

  • Cytoskeletal Proteins
  • MEFV protein, human
  • Peptide Fragments
  • Pyrin
  • Recombinant Fusion Proteins
  • polyhistidine
  • Histidine