Crystallization and preliminary X-ray analysis of human placental S-adenosylhomocysteine hydrolase.


Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Turner, MA; Dole, K; Yuan, CS; Hershfield, MS; Borchardt, RT; Howell, PL

Published Date

  • May 1, 1997

Published In

Volume / Issue

  • 53 / Pt 3

Start / End Page

  • 339 - 341

PubMed ID

  • 15299942

Pubmed Central ID

  • 15299942

International Standard Serial Number (ISSN)

  • 0907-4449

Digital Object Identifier (DOI)

  • 10.1107/S0907444996014746


  • eng

Conference Location

  • United States