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 unknown function. Its homologues are well conserved among both the eubacteria and the archaea. It has been overexpressed in soluble form in Escherichia coli. The protein has been crystallized at 296 K using 2-propanol as a precipitant. X-ray diffraction data have been collected to 1.9 A resolution using synchrotron radiation. The crystals belong to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 115.96, c = 78.60 A, alpha = beta = 90, gamma = 120 degrees. The asymmetric unit contains two monomers of the surE protein, with a corresponding V(M) of 2.72 A(3) Da(-1) and a solvent content of 54.7%.
Kwak
J E
JE
School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.
Ha
K S
KS
Lee
J Y
JY
Im
Y J
YJ
Park
S H
SH
Eom
S H
SH
Suh
S W
SW
D019840:2-Propanol; D000135:Acid Phosphatase; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D020124:Thermotoga maritima / Q000737:chemistry*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D000135:Acid Phosphatase; C089634:umpG protein, E coli; D019840:2-Propanol