title: Crystallization of parasporin-2, a Bacillus thuringiensis crystal protein with selective cytocidal activity against human cells.
abstract: Bacillus thuringiensis is a valuable source of protein toxins that are specifically effective against certain insects and worms but harmless to mammals. In contrast, a protein toxin obtained from B. thuringiensis strain A1547, designated parasporin-2, is not insecticidal but has a strong cytocidal activity against human cells with markedly divergent target specificity. The 37 kDa inactive protein is proteolytically activated to a 30 kDa active form. The active form of the recombinant protein toxin was crystallized in the presence of ethylene glycol and polyethylene glycol 8000 at neutral pH. The crystals belong to the hexagonal space group P6(1) or P6(5), with unit-cell parameters a = b = 134.37, c = 121.24 A. Diffraction data from a native crystal were collected to 2.75 A resolution using a synchrotron-radiation source.
authors.affiliation: Biological Information Research Center, AIST, Tsukuba, Ibaraki 305-8566, Japan.
authors.forename: Toshihiko
authors.initials: T
authors.lastname: Akiba
authors.forename: Yuichi
authors.initials: Y
authors.lastname: Abe
authors.forename: Sakae
authors.initials: S
authors.lastname: Kitada
authors.forename: Yoshitomo
authors.initials: Y
authors.lastname: Kusaka
authors.forename: Akio
authors.initials: A
authors.lastname: Ito
authors.forename: Tokio
authors.initials: T
authors.lastname: Ichimatsu
authors.forename: Hideki
authors.initials: H
authors.lastname: Katayama
authors.forename: Tetsuyuki
authors.initials: T
authors.lastname: Akao
authors.forename: Kazuhiko
authors.initials: K
authors.lastname: Higuchi
authors.forename: Eiichi
authors.initials: E
authors.lastname: Mizuki
authors.forename: Michio
authors.initials: M
authors.lastname: Ohba
authors.forename: Ryuta
authors.initials: R
authors.lastname: Kanai
authors.forename: Kazuaki
authors.initials: K
authors.lastname: Harata
mesh_terms: D001413:Bacillus thuringiensis / Q000737:chemistry* / Q000378:metabolism; D001427:Bacterial Toxins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D004731:Endotoxins / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism; D006639:Histidine / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D008715:Methionine / Q000737:chemistry; D009842:Oligopeptides / Q000737:chemistry; D011092:Polyethylene Glycols / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014961:X-Ray Diffraction
chemical_list: D001427:Bacterial Toxins; D004731:Endotoxins; C471213:His-His-His-His-His-His; D009842:Oligopeptides; D011506:Proteins; D011994:Recombinant Proteins; C412914:parasporin; D011092:Polyethylene Glycols; D006639:Histidine; D008715:Methionine