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Crystallization and low temperature diffraction studies of the DNA binding domain of the single-stranded DNA binding protein from Escherichia coli

Journal Article


Abstract


  • The DNA binding domain of the single-stranded DNA binding protein from Escherichia coli has been overproduced, purified and crystallized in a form suitable for X-ray diffraction studies. Crystals were produced by dialysis against low ionic strength buffer at high pH. The crystals belong to space group I222 or I21,21,21, with a = 82.47 Å, b = 65.27 Å and c = 46.50 Å. Data were collected at several temperatures and a significant improvement in data duality was observed with a decrease in temperature. On occasion, with the decrease in temperature, a transformation to a primitive space group was observed and temperature appears to play a key role in this transformation. A complete native data set has been collected to 2.57 Å at -15°C. © 1994 Academic Press Limited.

Publication Date


  • 1994

Citation


  • Thorn, J. M., Carr, P. D., Chase, J. W., Dixon, N. E., & Ollis, D. L. (1994). Crystallization and low temperature diffraction studies of the DNA binding domain of the single-stranded DNA binding protein from Escherichia coli. Journal of Molecular Biology, 240(4), 396-399. doi:10.1006/jmbi.1994.1453

Scopus Eid


  • 2-s2.0-0027935509

Start Page


  • 396

End Page


  • 399

Volume


  • 240

Issue


  • 4

Abstract


  • The DNA binding domain of the single-stranded DNA binding protein from Escherichia coli has been overproduced, purified and crystallized in a form suitable for X-ray diffraction studies. Crystals were produced by dialysis against low ionic strength buffer at high pH. The crystals belong to space group I222 or I21,21,21, with a = 82.47 Å, b = 65.27 Å and c = 46.50 Å. Data were collected at several temperatures and a significant improvement in data duality was observed with a decrease in temperature. On occasion, with the decrease in temperature, a transformation to a primitive space group was observed and temperature appears to play a key role in this transformation. A complete native data set has been collected to 2.57 Å at -15°C. © 1994 Academic Press Limited.

Publication Date


  • 1994

Citation


  • Thorn, J. M., Carr, P. D., Chase, J. W., Dixon, N. E., & Ollis, D. L. (1994). Crystallization and low temperature diffraction studies of the DNA binding domain of the single-stranded DNA binding protein from Escherichia coli. Journal of Molecular Biology, 240(4), 396-399. doi:10.1006/jmbi.1994.1453

Scopus Eid


  • 2-s2.0-0027935509

Start Page


  • 396

End Page


  • 399

Volume


  • 240

Issue


  • 4