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Crystals of glutathione transferase zeta 1 were grown and shown to diffract X-rays to 3.1 Å resolution. They belonged to space group P1, with unit-cell parameters a = 42.0, b = 49.6, c = 54.6 Å, α = 82.9, β = 69.9, γ = 73.4°.

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A controversy has existed in the literature between crystallographic and spectroscopic data on the binding mode of cyanate to carbonic anhydrase II (CA II). To settle this ambiguity, the X-ray crystal structures of the complexes of wild-type and V207I variant CA II with cyanate were redetermined to 1.7 and 1.5 Å resolution, respectively. The data clearly support that cyanate binds directly to the catalytic zinc and not as an outer sphere ligand mimicking the binding of CO2.
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