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

Hajime Sugawara, Tomoyuki Yamaya, Hitoshi Sakakibara

Research output: Contribution to journalArticle

3 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)366-368
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume61
Issue number4
DOIs
Publication statusPublished - 2005 Dec 1
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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