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The role of monovalent cations in the ATPase reaction of DNA gyrase

Four new crystal structures of the ATPase domain of the GyrB subunit of Escherichia coli DNA gyrase have been determined. One of these, solved in the presence of K(+), is the highest resolution structure reported so far for this domain and, in conjunction with the three other structures, reveals new...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Julkaisussa:Acta Crystallogr D Biol Crystallogr
Päätekijät: Hearnshaw, Stephen James, Chung, Terence Tsz-Hong, Stevenson, Clare Elizabeth Mary, Maxwell, Anthony, Lawson, David Mark
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: International Union of Crystallography 2015
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC4388272/
https://ncbi.nlm.nih.gov/pubmed/25849408
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1399004715002916
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