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Crystallization and preliminary X-ray diffraction study of the histidine-containing phosphotransfer protein ZmHP1 from maize
- Source :
- Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 4)
- Publication Year :
- 2004
-
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.
- Subjects :
- Biophysics
Polyethylene glycol
Biochemistry
Zea mays
law.invention
Polyethylene Glycols
chemistry.chemical_compound
X-Ray Diffraction
Structural Biology
law
Genetics
Histidine
Crystallization
Cloning, Molecular
Plant Proteins
Resolution (electron density)
Histidine kinase
Space group
Condensed Matter Physics
Response regulator
Crystallography
Phosphotransferases (Alcohol Group Acceptor)
chemistry
Crystallization Communications
X-ray crystallography
biological sciences
health occupations
bacteria
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 61
- Issue :
- Pt 4
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Accession number :
- edsair.doi.dedup.....f48bebd72a516f9dffe6ce3c80612b64