Activity of the 20S proteasome, which performs much of the cytosolic a
nd nuclear proteolysis in eukaryotic cells, is controlled by regulator
y complexes that bind to one or both ends of the cylindrical proteasom
e. One of these complexes, the 11S regulator (REG), is a complex of 28
kDa subunits that is thought to activate proteasomes toward the produ
ction of antigenic peptides. REG, purified from red blood cells, is a
complex of REG alpha and REG beta subunits. We have crystallized recom
binant REG alpha (rREG alpha) and collected diffraction data to 3.0 An
gstrom resolution. The self-rotation function indicates that rREG alph
a forms a heptameric ring in the crystal. Equilibrium sedimentation de
monstrates that rREG alpha is a heptamer in solution also.