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The crystal structures of two forms of the enzyme (native and inhibited by chloride) were studied by X-ray diffraction analysis. This allowed us to obtain the structural data necessary for understanding the mechanism of enzymatic activity of the dimanganese catalase.
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This page is a summary of: Three-dimensional structure of the enzyme dimanganese catalase from Thermus Thermophilus at 1 Å resolution, Crystallography Reports, January 2000, Pleiades Publishing Ltd,
DOI: 10.1134/1.171145.
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