The binding of transcription factor ATF-1 to DNA contributes to gene expres
sion and regulation of cell growth. Antibody Mab41.4, raised against ATF-1,
and its derivatives Fab41.4 and scFv41.4 inhibit specific DNA binding in v
itro and induce apoptotic death of tumor cells in vivo. Structural studies
of Fab41.4 were performed to gain insight into the mechanism of action of t
his potentially therapeutic antibody. The optimal conditions for crystalliz
ation of Fab41.4 were determined. Crystals were needle-like in appearance,
displayed C2 space-group symmetry and diffracted to a resolution of 1.6 Ang
strom. The unit-cell parameters were determined to be a = 186.64, b = 40.22
, c = 55.58 Angstrom, alpha = gamma = 90, beta = 96.93 degrees. The data se
t was 97.7% complete. Molecular replacement was performed, resulting in an
R value of 44.6%.