title: Crystallization and preliminary X-ray crystallographic study of the ribosomal protein S7 from Bacillus stearothermophilus.
abstract: Overproduction and crystallization of Bacillus stearothermophilus ribosomal protein S7 (BstS7), a primary 16S rRNA binding protein and also a translational repressor protein, have been performed to analyze its three-dimensional structure by X-ray crystallography. Ribosomal protein BstS7 was expressed in the cytoplasmic fraction of the E. coli cells and purified to homogeneity. This recombinant BstS7 was used to produce crystals with P2(1) symmetry that diffracted to 2.5 A resolution which are suitable for high-resolution X-ray crystallographic analysis.
authors.affiliation: Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
authors.forename: N
authors.initials: N
authors.lastname: Harada
authors.forename: K
authors.initials: K
authors.lastname: Sano
authors.forename: M
authors.initials: M
authors.lastname: Kimura
authors.forename: H
authors.initials: H
authors.lastname: Hosaka
authors.forename: A
authors.initials: A
authors.lastname: Nakagawa
authors.forename: I
authors.initials: I
authors.lastname: Tanaka
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D001411:Geobacillus stearothermophilus; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D011994:Recombinant Proteins; D012269:Ribosomal Proteins; C037442:ribosomal protein S7