Crystallization and preliminary X-ray diffraction study of the histidine-containing phosphotransfer protein ZmHP1 from maize

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Hajime SugawaraHitoshi Sakakibara

Abstract

In histidine-aspartate phosphorelays (two-component systems) involved in plant-hormone signalling, histidine-containing phosphotransfer (HPt) proteins mediate the transfer of a phosphoryl group from the sensory histidine kinase to the response regulator. The maize HPt protein ZmHP1 has been crystallized. Although ZmHP1 with an N-terminal His tag could be crystallized using sodium chloride as a precipitant, the crystals diffracted poorly to only 3.2 A resolution. When the His tag was removed, ZmHP1 crystals were obtained using polyethylene glycol 4000 as a precipitant and the diffraction data were greatly enhanced to 2.4 A resolution. The crystals belonged to the space group P4(1)2(1)2, with one ZmHP1 molecule in the asymmetric unit.

References

Apr 28, 1968·Journal of Molecular Biology·B W Matthews
Oct 26, 1999·Acta Crystallographica. Section D, Biological Crystallography·M G Rossmann, C G van Beek
Aug 31, 2000·Annual Review of Biochemistry·A M StockP N Goudreau
Jun 18, 2002·Plant Physiology·Ildoo HwangJen Sheen
Sep 25, 2003·Annual Review of Plant Biology·Tatsuo Kakimoto
Dec 4, 2004·Protein Science : a Publication of the Protein Society·Hajime SugawaraHitoshi Sakakibara

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Citations

Jun 15, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Ruhu QiAaron J Oakley
Jul 7, 2015·Acta Crystallographica. Section F, Structural Biology Communications·Bostjan KobeSimon J Williams
Nov 4, 2010·Plant Signaling & Behavior·Eva HellmannAlexander Heyl

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