Je. Kwak et al., Crystallization and preliminary X-ray crystallographic analysis of the surE protein from Thermotoga maritima, ACT CRYST D, 57, 2001, pp. 612-613
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%.