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Crystallization and X-ray diffraction analysis of the DNA-remodelling protein DnaD from Bacillus subtilis

Journal Article · · Acta Crystallographica. Section F
 [1]; ;  [2];  [1]
  1. School of Pharmacy and Centre for Biomolecular Sciences, University of Nottingham (United Kingdom)
  2. School of Chemistry and Centre for Biomolecular Sciences, University of Nottingham (United Kingdom)
Crystallization and preliminary X-ray diffraction analysis of the two domains of DnaD from B. subtilis is reported. The DnaD protein is an essential component of the chromosome-replication machinery of the Gram-positive bacterium Bacillus subtilis and is part of the primosomal cascade that ultimately loads the replicative ring helicase DnaC onto DNA. Moreover, DnaD is a global regulator of DNA architecture, as it forms higher order nucleoprotein structures in order to open supercoiled DNA. Here, the crystallization and preliminary X-ray diffraction analysis of the two domains of DnaD from B. subtilis are reported. Crystals of the N-terminal domain are trigonal, with either P3{sub 1}21 or P3{sub 2}21 space-group symmetry, and diffracted X-rays to 2.0 Å resolution; crystals of the C-terminal domain are hexagonal, with space group P6{sub 1} or P6{sub 5}, and diffracted X-rays to 2.9 Å resolution in-house. Determination of the structure of the DnaD domains will provide insight into how remodelling of the nucleoid is associated with priming of replication in the model Gram-positive organism B. subtilis.
OSTI ID:
22360266
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 2 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English

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