A novel approach to studying the structural and functional properties of proteins with unknown functions
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Three proteins from extremophilic bacteria—hypothetical monooxygenase from Deinococcus radiodurans, hypothetical nucleotidyl transferase from Thermotoga maritime, and hypothetical oxidoreductase from Exiguobacterium sibiricum—and the DJ-1 chaperone protein from Homo sapiens have been produced in Escherichia coli. The isolation and purification procedures developed for the recombinant proteins allowed us to achieve yields higher than 96%. Crystallization conditions enabling stable growth of crystals have been determined. X-ray experiments have been performed to test the quality of the crystals and the resolution achieved ranged from 1.2 to 1.8 Å.
Keywordsunknown ligands crystallization X-ray structure analysis
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