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One of the zinc ligands in human carbonic anhydrase II, His 94 , has been replaced with glutamic acid by site-directed mutagenesis. The mutation leads to a less stable zinc binding site and to significant non-local perturbations of the protein structure. The crystals are composed of a mixture of holo- and apoenzyme, and the side chain of Glu 94 has two conformations. In the...
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