ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
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 Å, α = β = γ = 90°. The crystals exhibit the symmetry of space group C222 and diffract to a minimum spacing of ∼ 2.0 Å 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 Å3 Da−l). The self-rotation function clearly indicates the location of the non-crystallographic twofold axis.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0907444996014746
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