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Preliminary crystallographic analysis of the breakage-reunion domain of the Escherichia coli DNA gyrase A protein.

Abstract：

: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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Reece RJ,Dauter Z,Wilson KS,Maxwell A,Wigley DB

doi

10.1016/S0022-2836(05)80162-7

subject

Has Abstract

pub_date

1990-10-20 00:00:00

pages

493-5

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)80162-7

journal_volume

215

pub_type

杂志文章

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