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Updated: Jan 23, 2026
Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies
Published on: April 11, 2021
Crystallization and preliminary X-ray diffraction study of the histidine-containing phosphotransfer protein ZmHP1
Hajime Sugawara1, Tomoyuki Yamaya, Hitoshi Sakakibara
1Laboratory for Communication Mechanisms, RIKEN Plant Science Center, Yokohama 230-0045, Japan. sugawara@psc.riken.go.jp
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.
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