Crystallization and preliminary X‐ray crystallographic studies of human FAIM protein

Fas apoptosis inhibitory molecule (FAIM), an antagonist of Fas‐induced cell death, is highly conserved and is broadly expressed in many tissues. It has been found that FAIM can stimulate neurite outgrowth in PC12 cells and primary neurons. However, the molecular mechanisms of action of FAIM are not understood in detail. Here, full‐length human FAIM and two truncation constructs have successfully been cloned, expressed and purified in Escherichia coli . FAIM (1–90) was crystallized and diffracted to a resolution of 2.5 Å; the crystal belonged to space group P 3 1 , with unit‐cell parameters a = b = 58.02, c  = 71.11 Å, α = β = 90, γ = 120°. There were two molecules in the asymmetric unit.