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Crystallization and preliminary X-ray analysis of human placental S-adenosylhomocysteine hydrolase
Turner, Mary A. Dole, Kiran Yuan, Chong-Sheng Hershfield, Michael S. Borchardt, Ronald T. Howell, P. Lynne
Turner, Mary A.
Dole, Kiran
Yuan, Chong-Sheng
Hershfield, Michael S.
Borchardt, Ronald T.
Howell, P. Lynne
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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 fiat plates, with unit-cell dimensions a=96.2, b=173.6, c=142.9A, ct=fl=7=90 °. The crystals exhibit the symmetry of space group C222 and diffract to a minimum spacing of "-~ 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 (Vm = 2.99 ,~3 Da-l). The selfrotation function clearly indicates the location of the noncrystallographic twofold axis.
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1997
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International Union of Crystallography
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Turner, M.A. et al. "Crystallization and preliminary X-ray analysis of human placental S-adenosylhomocysteine hydrolase." Acta Cryst. (1997). D53, 339-341 http://dx.doi:10.org/1107/S0907444996014746