Abstract
The DbeA1 variant of a novel haloalkane dehalogenaseDbeA (EC 3.8.1.5) from Bradyrhizobium elkani USDA94 was constructed to study the structure-function relationships between DbjA and DbeA enzymes. A DbeA1 variant carries a unique fragment of nine amino acids transplanted from the sequentially closely related enzyme DbjA from Bradyrhizobium japonicum USDA110 to DbeA. Here we report development of the crystallization protocol for DbeA1 and soaking experiments with the ligands 1-fluoropentane and 1,3-dichloropropane.
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