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The crystallization and preliminary X-ray diffraction analysis of a novel chloromuconolactone dehalogenase from R. opacus 1CP are described. The oligomeric state was determined based on the self-rotation function.

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The crystallization of human ecto-5'-nucleotidase (CD73) paves the way for detailed studies of the domain motion between the open and closed forms. It will also enable the structure-based design of inhibitors targeting the open form.
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