Acta Crystallographica Section F 2013-03-01

Crystallization and preliminary X-ray crystallographic studies of cPOP1.

Kyung Hoon Do, Hyun Ho Park

Index: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 69(Pt 3) , 292-4, (2013)

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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°.

Related Compounds

  • L-Histidine
  • Poly-L-histidine

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