Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the receiver domain of PhoB

Citation
M. Sola et al., Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the receiver domain of PhoB, ACT CRYST D, 54, 1998, pp. 1460-1463
Citations number
23
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
54
Year of publication
1998
Part
6
Pages
1460 - 1463
Database
ISI
SICI code
0907-4449(19981101)54:S2<1460:OPCAPX>2.0.ZU;2-B
Abstract
PhoB is the response regulator of the E. coli two-component signal transduc tion system for phosphate regulation. It is a transcription factor that act ivates more than 30 genes of the pho regulon. Crystals of the receiver doma in of PhoB were obtained by applying the hanging-drop vapour-diffusion meth od. X-ray diffraction data have been collected using synchrotron radiation to 1.88 Angstrom resolution. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell constants a = 34.11, b = 60.42, c = 119. 97 Angstrom. The Matthews parameter suggests that PhoB crystallizes with tw o molecules per asymmetric unit, suggesting that activating dimerization oc curs in the crystal.