Crystallization and preliminary X-ray crystallographic analysis of the surE protein from Thermotoga maritima

The surE protein from Thermotoga maritima is a 247-residue protein of unkno wn function. Its homologues are well conserved among both the eubacteria an d the archaea. It has been overexpressed in soluble form in Escherichia col i. The protein has been crystallized at 296 K using 2-propanol as a precipi tant. X-ray diffraction data have been collected to 1.9 Angstrom resolution using synchrotron radiation. The crystals belong to the trigonal space gro up P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 115.96, c = 78.6 0 Angstrom, alpha = beta = 90, gamma = 120 degrees. The asymmetric unit con tains two monomers of the surE protein, with a corresponding V-M of 2.72 An gstrom (3) Da(-1) and a solvent content of 54.7%.