Open AccessCrystallization and preliminary X‐ray diffraction analysis of two N‐terminal fragments of the DNA‐cleavage domain of topoisomerase IV from Staphylococcus aureus
Author(s) -
Carr Stephen B.,
Makris George,
Phillips Simon E. V.,
Thomas Christopher D.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106044150
Subject(s) - cleavage (geology) , topoisomerase , crystallography , crystallization , dna , x ray crystallography , chemistry , molecule , diffraction , stereochemistry , biology , biochemistry , physics , optics , organic chemistry , fracture (geology) , paleontology
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 crystallized. Crystals were grown at 291 K using the sitting‐drop vapour‐diffusion technique with PEG 3350 as a precipitant. Preliminary X‐ray analysis revealed that GrlA56 crystals belong to space group P 2 1 , diffract to a resolution of 2.9 Å and possess unit‐cell parameters a = 83.6, b = 171.5, c = 87.8 Å, β = 90.1°, while crystals of GrlA59 belong to space group P 2 1 2 1 2, with unit‐cell parameters a = 41.5, b = 171.89, c = 87.9 Å. These crystals diffract to a resolution of 2.8 Å. This is the first report of the crystallization and preliminary X‐ray analysis of the DNA‐cleavage domain of a topoisomerase IV from a Gram‐positive organism.