Crystal structure of an N-terminal fragment of the DNA gyrase B protein

@article{Wigley1991CrystalSO,
  title={Crystal structure of an N-terminal fragment of the DNA gyrase B protein},
  author={Dale B. Wigley and Gideon J. Davies and Eleanor J. Dodson and Anthony Maxwell and Guy G. Dodson},
  journal={Nature},
  year={1991},
  volume={351},
  pages={624-629}
}
The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, com-plexed with a nonhn/drolysable ATP analogue, has been solved at 2.5 Å resolution. It consists of two domains, both containing novel protein folds. The protein fragment forms a dimer, whose N-terminal domains are responsible for ATP binding and hydrolysis. The C-terminal domains form the sides of a 20 Å hole through the protein dimer which may play a role in DNA strand passage during the… 
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TLDR
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TLDR
The 24 kDa fragment of DNA gyrase B from Staphylococcus aureus was expressed in Escherichia coli and purified for crystallization and the most stable mutants produced crystals.
The C-terminal domain of DNA gyrase A adopts a DNA-bending β-pinwheel fold
TLDR
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Backbone assignment of the N-terminal 24-kDa fragment of Escherichia coli topoisomerase IV ParE subunit
TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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