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

Citation
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
Citations number
9
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
57
Year of publication
2001
Part
4
Pages
612 - 613
Database
ISI
SICI code
0907-4449(200104)57:<612:CAPXCA>2.0.ZU;2-5
Abstract
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%.