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

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.