A novel approach to studying the structural and functional properties of proteins with unknown functions
| Autor: | A. G. Yarosh, I.A. Shumilin, K. M. Boiko, M.A. Gorbacheva, A. V. Lipkin, D. A. Korzhenevskii, Vladimir Popov, Pavel V. Dorovatovskii, Tatiana V. Rakitina |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
chemistry.chemical_classification
biology Organic Chemistry Deinococcus radiodurans Thermotoga biology.organism_classification Exiguobacterium medicine.disease_cause Biochemistry law.invention chemistry Oxidoreductase law Recombinant DNA medicine bacteria Bioorganic chemistry Transferase Escherichia coli |
| Zdroj: | Russian Journal of Bioorganic Chemistry. 38:83-88 |
| ISSN: | 1608-330X 1068-1620 |
| DOI: | 10.1134/s1068162012010098 |
| Popis: | 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 A. |
| Databáze: | OpenAIRE |
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