Preliminary crystallographic analysis of the breakage-reunion domain of the Escherichia coli DNA gyrase A protein.
The 64 x 10(3) Mr N-terminal breakage-reunion domain of the Escherichia coli DNA gyrase A protein was purified from an over-expressing strain. When complexed with the gyrase B protein, this truncated A protein has all of the enzymic properties of the full-length counterpart, although with reduced efficiency in some cases. The 64 x 10(3) Mr protein has been crystallized in several forms, a number of which were too small for crystallographic analysis. However, two forms grew to sufficient size for preliminary X-ray analysis. Both forms were tetragonal with a primitive lattice. One form (type I) had cell dimensions of a = b = 170 A, c = 145 A a space group of either P41212 (P43212) or P42212, and diffracted to 6 A resolution. The type II crystals had cell dimensions of a = b = 177 A, c = 175 A, a space group of P41212 (P43212) or P42212, and diffracted to at least 4.5 A resolution. Both crystal forms apparently contained four subunits (possibly a tetramer) in the asymmetric unit. We are attempting to increase the size and quality of these crystals.
Reece
R J
RJ
Department of Biochemistry, University of Leicester, U.K.
Dauter
Z
Z
Wilson
K S
KS
Maxwell
A
A
Wigley
D B
DB
D004250:DNA Topoisomerases, Type II / Q000737:chemistry* / Q000378:metabolism; D004269:DNA, Bacterial / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D008970:Molecular Weight; D011489:Protein Denaturation; D014961:X-Ray Diffraction
D004269:DNA, Bacterial; D004250:DNA Topoisomerases, Type II