title: Crystallization and preliminary X-ray diffraction studies of HutP protein: an RNA-binding protein that regulates the transcription of hut operon in Bacillus subtilis.
abstract: 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. HutP and its mutant, 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 dimensions a=b=c=95.6A for HutP and a=b=c=96.8A for the mutant. Complete data sets of 3.0-A resolution for wild-type HutP and of 2.70-A resolution for the mutant HutP were collected.
authors.affiliation: Institute of Molecular and Cell Biology, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 6, Tsukuba, Ibaraki 305-8566, Japan.
authors.forename: T S
authors.initials: TS
authors.lastname: Kumarevel
authors.forename: Z
authors.initials: Z
authors.lastname: Fujimoto
authors.forename: B
authors.initials: B
authors.lastname: Padmanabhan
authors.forename: M
authors.initials: M
authors.lastname: Oda
authors.forename: S
authors.initials: S
authors.lastname: Nishikawa
authors.forename: H
authors.initials: H
authors.lastname: Mizuno
authors.forename: P K R
authors.initials: PK
authors.lastname: Kumar
mesh_terms: D001412:Bacillus subtilis / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D009876:Operon; D016601:RNA-Binding Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods*
chemical_list: D001426:Bacterial Proteins; D016601:RNA-Binding Proteins