Purification and preliminary crystallographic studies on the sporulation response regulatory phosphotransferase protein, Spo0B, from Bacillus subtilis.
The phosphotransferase protein Spo0B, a component of the sporulation signal transduction system in Bacillus subtilis was expressed from the Escherichia coli strain BL21DE3. It was purified, crystallized, and 2.25 A data measured using the synchrotron source at the Stanford Linear Accelerator Center. The search for heavy atom derivatives is in progress.
Zhou
X Z
XZ
Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, California 92037, USA.
Madhusudan
Whiteley
J M
JM
Hoch
J A
JA
Varughese
K I
KI
D001412:Bacillus subtilis / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D010770:Phosphotransferases / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry; D012808:Sigma Factor; D015398:Signal Transduction; D013171:Spores, Bacterial / Q000201:enzymology; D017356:Synchrotrons; D014157:Transcription Factors
D001426:Bacterial Proteins; D011994:Recombinant Proteins; D012808:Sigma Factor; D014157:Transcription Factors; C092468:spoIIR protein, Bacillus subtilis; C030069:spore-specific proteins, Bacillus; D010770:Phosphotransferases