Crystallization and preliminary X-ray diffraction study of the histidine-containing phosphotransfer protein ZmHP1 from maize
- Laboratory for Communication Mechanisms, RIKEN Plant Science Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045 (Japan)
The histidine-containing phosphotransfer protein ZmHP1 from maize was crystallized. The removal of an N-terminal His tag resulted in a remarkable improvement of the diffraction data. 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 P4{sub 1}2{sub 1}2, with one ZmHP1 molecule in the asymmetric unit.
- OSTI ID:
- 22356121
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 4; Other Information: PMCID: PMC1952433; PMID: 16511042; PUBLISHER-ID: vr5025; OAI: oai:pubmedcentral.nih.gov:1952433; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Distribution and evolution of multiple-step phosphorelay in prokaryotes: lateral domain recruitment involved in the formation of hybrid-type histidine kinases
Imidazole as a Small Molecule Analogue in Two-Component Signal Transduction