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To study enzyme functionality, two haloalkane dehalogenase variants LinB32 and LinB70 carrying single-point and double-point mutations were constructed and crystallized in different crystallization conditions. Both LinB variants and their complexes with halogenated substrates diffracted to resolutions ranging from 1.6 to 2.8 Å.

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The novel haloalkane dehalogenases DpcA from P. cryohalolentis K5 and DmxA from Marinobacter sp. ELB17 were successfully crystallized and diffraction data were collected to resolutions of 1.05 and 2.49 Å, respectively.
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