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

J Mol Biol. 1994 Jul 22;240(4):396-9. doi: 10.1006/jmbi.1994.1453.

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(1)2(1)2(1) with a = 82.47 A, b = 65.27 A and c = 46.50 A. 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 A at -15 degrees C.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Base Sequence
  • Binding Sites
  • Cold Temperature
  • Crystallography, X-Ray
  • DNA, Single-Stranded
  • DNA-Binding Proteins / chemistry*
  • Escherichia coli / chemistry*
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides

Substances

  • Bacterial Proteins
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Oligodeoxyribonucleotides