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Crystallization and Low Temperature Diffraction Studies of the DNA Binding Domain of the Single-stranded DNA Binding Protein fromEscherichia coli

Authors
Journal
Journal of Molecular Biology
0022-2836
Publisher
Elsevier
Publication Date
Volume
240
Issue
4
Identifiers
DOI: 10.1006/jmbi.1994.1453
Keywords
  • Single-Stranded Binding Protein
  • Purification
  • Crystallization
  • X-Ray Diffraction
  • Low Temperature
Disciplines
  • Biology

Abstract

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 I2 12 12 1 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 quality 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.

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