title: Crystallization and preliminary X-ray crystallographic studies of human FAIM protein.
abstract: 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 A; the crystal belonged to space group P3(1), with unit-cell parameters a=b=58.02, c=71.11 A, alpha=beta=90, gamma=120 degrees. There were two molecules in the asymmetric unit.
authors.affiliation: School of Biological Science and Medical Engineering, Beihang University, Beijing 100191, People's Republic of China.
authors.forename: Guoming
authors.initials: G
authors.lastname: Li
authors.forename: Linglong
authors.initials: L
authors.lastname: Qu
authors.forename: Geng
authors.initials: G
authors.lastname: Meng
authors.forename: Xiaoyun
authors.initials: X
authors.lastname: Bai
authors.forename: Kesheng
authors.initials: K
authors.lastname: Dai
authors.forename: Xiaofeng
authors.initials: X
authors.lastname: Zheng
mesh_terms: D051017:Apoptosis Regulatory Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans
chemical_list: D051017:Apoptosis Regulatory Proteins; C421307:FAIM protein, human