Abstract
A recombinant form of human placental S-adenosylhomocysteine (AdoHcy) hydrolase expressed in E. coli, which was inactivated by a type-I mechanism-based inhibitor, has been crystallized using the hanging-drop vapour-diffusion technique. The crystals grow as flat plates, with unit-cell dimensions a = 96.2, b = 173.6, c = 142.9 A, alpha = beta = gamma = 90 degrees. The crystals exhibit the symmetry of space group C222 and diffract to a minimum spacing of approximately 2.0 A resolution at the Cornell High Energy Synchrotron Source. On the basis of density calculations two monomers of the tetrameric protein are estimated to be present in the asymmetric unit (V(m) = 2.99 A(3) Da(-l)). The self-rotation function clearly indicates the location of the non-crystallographic twofold axis.
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