| Autor: |
Mi Li, Gustchina, Alla, Rasulova, Fatima S., Melnikov, Edward E., Maurizi, Michael R., Rotanova, Tatyana V., Dauter, Zbigniew, Wlodawer, Alexander |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section D (Wiley-Blackwell); Aug2010, Vol. 66 Issue 8, p865-873, 9p, 5 Diagrams, 3 Charts |
| Abstrakt: |
The article presents information on a research study which examined the structural properties of the N-terminal fragment of Escherichia coli Lon protease. For the study, researchers used a two-step process for moving a clone of intact Escherichia coli Lon from plasmid pLon500 to the pET30a vector. They determined the structure of Lon-N245 through a single-wavelength anomolous diffraction of crystals of selenomethionine-containing protein. A comparison of the Lon structure with other putative substrate-binding domains of proteins is provided. |
| Databáze: |
Complementary Index |
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