Crystallization and preliminary X-ray diffraction studies of HutP protein: an RNA-binding protein that regulates the transcription of hut operon in Bacillus subtilis.
HutP is an RNA-binding protein and regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences on hut mRNA. A single point mutant (Val51Ile), which has increased affinity for the regulatory sequences, were purified and crystallized by the hanging drop vapor diffusion method. The space group was P2(1)3 with unit cell dimension a = b = c = 95.60 A resolution, and contain two molecules in the asymmetric unit. A complete MAD data set of 3.0 A resolution were collected at the LIII edge of Hg.
Kumarevel
Thirumananseri
T
Institute of Molecular and Cell Biology, National Institute of Advanced Industrial Science and Technology, Department of Biotechnology, National Institute of Agrobiological Resources, Tsukuba, Ibaraki, Japan.
Fujimoto
Zui
Z
Oda
Masanao
M
Nishikawa
Satoshi
S
Mizuno
Hiroshi
H
Kumar
Penmetcha K
PK
D001412:Bacillus subtilis / Q000235:genetics*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D009876:Operon; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D014158:Transcription, Genetic / Q000502:physiology*
D016601:RNA-Binding Proteins