Open AccessCrystallization and preliminary X‐ray diffraction study of the histidine‐containing phosphotransfer protein ZmHP1 from maize
Author(s) -
Yamaya Tomoyuki,
Sugawara Hajime,
Sakakibara Hitoshi
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105006846
Subject(s) - histidine , crystallization , polyethylene glycol , crystallography , resolution (logic) , chemistry , molecule , sodium , protein crystallization , biochemistry , enzyme , organic chemistry , artificial intelligence , computer science
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 P 4 1 2 1 2, with one ZmHP1 molecule in the asymmetric unit.