PMID:12351839
| Citation |
Shindoh, K, Maenaka, K, Akiba, T, Okamura, H, Nishimura, Y, Makino, K and Shirakihara, Y (2002) Crystallization and preliminary X-ray diffraction studies on the DNA-binding domain of the transcriptional activator protein PhoB from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 58:1862-4 |
|---|---|
| Abstract |
PhoB is a transcriptional factor that activates more than 30 genes of the pho regulon in response to phosphate starvation. Crystals of its C-terminal domain (PhoBC) were obtained in two forms. The first crystal form, obtained from phosphate solution, belongs to space group P2(1), with unit-cell parameters a = 30.7, b = 105.9, c = 30.9 A, beta = 110.3 degrees. The second form, crystallized from PEG solution, belongs to the same space group, but has a smaller unit cell (a = 30.6, b = 37.5, c = 44.4 A, beta = 109.4 degrees ). Crystals of selenomethionyl-derivatized PhoBC were obtained using the conditions for the second crystal form. Diffraction data from wild-type PhoBC (2.0 A resolution) and MAD data sets from selenomethionyl-derivative PhoBC (3.0 A resolution) have been collected at 100 K with a synchrotron-radiation source. MAD data analysis is in progress. |
| Links | |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Crystallization; Crystallography, X-Ray/methods; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/isolation & purification; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Polyethylene Glycols; Protein Isoforms/chemistry; Protein Isoforms/isolation & purification |
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