Crystallization and preliminary X-ray crystallographic analysis of the TM1442 gene product from Thermotoga maritima, a homologue of Bacillus subtilis anti-anti-sigma factors.
A 110-residue protein encoded by the TM1442 gene of Thermotoga maritima shows amino-acid sequence similarity to Bacillus subtilis anti-anti-sigma factors RsbV and SpoIIAA. It has been overexpressed in Escherichia coli and the recombinant protein exists primarily as both a monomer and a dimer in solution. The dimeric form has been crystallized using polyethylene glycol (PEG) 8000 as a precipitant. Native X-ray diffraction data have been collected at 100 K to 2.0 A resolution. The crystals are monoclinic, belonging to the space group P2(1), with unit-cell parameters a = 31.54 (13), b = 116.83 (37), c = 31.39 (7) A, alpha = 90, beta = 119.84 (9), gamma = 90 degrees. The asymmetric unit contains two monomers of the recombinant polypeptide, with a corresponding V(M) of 2.24 A(3) Da(-1) and a solvent content of 45.0%.
Ha
K S
KS
School of Chemistry and Molecular Engineering, Seoul National University, Seoul 151-742, South Korea.
Kwak
J E
JE
Han
B W
BW
Lee
J Y
JY
Moon
J
J
Lee
B I
BI
Suh
S W
SW
D001412:Bacillus subtilis / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D005798:Genes, Bacterial; D011994:Recombinant Proteins / Q000737:chemistry; D012808:Sigma Factor; D020124:Thermotoga maritima / Q000235:genetics*; D014157:Transcription Factors
D001426:Bacterial Proteins; D011994:Recombinant Proteins; C086522:RsbV protein, Bacteria; D012808:Sigma Factor; D014157:Transcription Factors; C092468:spoIIR protein, Bacillus subtilis; C030069:spore-specific proteins, Bacillus