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

Hajime Sugawara, Tomoyuki Yamaya, Hitoshi Sakakibara

研究成果: Article査読

4 被引用数 (Scopus)

抄録

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 Å 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 Å resolution. The crystals belonged to the space group P41212, with one ZmHP1 molecule in the asymmetric unit.

本文言語English
ページ(範囲)366-368
ページ数3
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
61
4
DOI
出版ステータスPublished - 2005
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 遺伝学
  • 凝縮系物理学

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