SixA has been isolated from Escherichia coli as the first protein to exhibit phospho-histidine phosphatase activity. Recent biochemical studies have shown that SixA is involved in the signal transduction of the His-Asp phosphorelay through the dephosphorylation of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB. Crystals of SixA were obtained using a hanging-drop vapour-diffusion method with polyethylene glycol and calcium ions. Preliminary X-ray crystallographic analysis revealed that the crystals belonged to space group P212121 with unit-cell dimensions a = 39.26, b = 48.62 and c = 83.18 Å, having one molecule in the crystallographic asymmetric unit. The intensity data were collected up to 1.5 Å resolution using synchrotron radiation.
|Original language||English (US)|
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - Jan 1 1999|
ASJC Scopus subject areas
- Structural Biology