Crystallization and preliminary X-ray diffraction analysis of two N-terminal fragments of the DNA-cleavage domain of topoisomerase IV from Staphylococcus aureus

DNA topoisomerase IV removes undesirable topological features from DNA molecules in order to help maintain chromosome stability. Two constructs of 56 and 59 kDa spanning the DNA-cleavage domain of the A subunit of topoisomerase IV from Staphylococcus aureus (termed GrlA56 and GrlA59) have been cryst...

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Detalles Bibliográficos
Autores principales: Carr, Stephen B., Makris, George, Phillips, Simon E. V., Thomas, Christopher D.
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2006
Materias:
Crystallization Communications
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225206/
https://www.ncbi.nlm.nih.gov/pubmed/17077506
http://dx.doi.org/10.1107/S1744309106044150

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2225206/
https://www.ncbi.nlm.nih.gov/pubmed/17077506
http://dx.doi.org/10.1107/S1744309106044150

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