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 journalArticlepeer-review

    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

    ASJC Scopus subject areas

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

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