Crystallization and preliminary crystallographic analysis of the DNA gyrase B protein from  B. stearothermophilus | Zendy

Tsai F. T. F. | Zendy; Subramanya H. S. | Zendy; Brannigan J. A. | Zendy; Wilkinson A. J. | Zendy; Wigley D. B. | Zendy

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Crystallization and preliminary crystallographic analysis of the DNA gyrase B protein from B. stearothermophilus

Author(s) -

Tsai F. T. F.,

Subramanya H. S.,

Brannigan J. A.,

Wilkinson A. J.,

Wigley D. B.

Publication year - 1996

Publication title -

acta crystallographica section d

Language(s) - English

Resource type - Journals

ISSN - 1399-0047

DOI - 10.1107/s0907444996008979

Subject(s) - dna gyrase , crystallography , crystallization , dimer , chemistry , trimer , atom (system on chip) , dna , stereochemistry , biochemistry , escherichia coli , gene , organic chemistry , computer science , embedded system

DNA gyrase B (GyrB) from B. stearothermophilus has been crystallized in the presence of the non‐hydrolyzable ATP analogue, 5′‐adenylyl‐β‐γ‐imidodiphosphate (ADPNP), by the dialysis method. A complete native data set to 3.7 Å has been collected from crystals which belonged to the cubic space group I 23 with unit‐cell dimension a = 250.6 Å. Self‐rotation function analysis indicates the position of a molecular twofold axis. Low‐resolution data sets of a thimerosal and a selenomethionine derivative have also been analysed. The heavy‐atom positions are consistent with one dimer in the asymmetric unit.

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