Abstract
The C-terminal 232-419 amino acids fragment of endonuclease Sau3AI has been successfully expressed in Escherichia coli with 6 His at its N-terminal. After purification and crystallization, one completed 2.8 Å data set was collected using a Rigaku R-AXIS IV ++ diffractometer. The plate-like crystals belong to orthorhombic space group P212121 with the cell dimension of a = 34.75, b = 76.82, c = 123.59Å and contain one molecule per asymmetric unit.
Keywords: Sau3AI endonuclease, crystallization, preliminary X-ray analysis