title: Structure of a beheaded 30 S ribosomal subunit from Thermus thermophilus.
abstract: The 22 S ribonucleoproten particles containing the 5' (body) and the central (platform) domains of the Thermus thermophilus 30 S subunit has been studied by sedimentation, neutron scattering and electron microscopy. The RNP particles have been obtained by oligonucleotide-directed cleavage of 16 S RNA with ribonulease H in the region of the 900th nucleotide of the protein-deficient derivatives of the 30 S subunits. It is shown that these RNP particles are very compact, though their form and dimensions differ slightly from those expected from the electron microscopy model of the 30 S subunit beheaded by computer simulation. The particles are subdivided into two structural domains whose mutual arrangement differs from that of the corresponding morphological parts of the native 30 S subunit. Electron microscopy demonstrates that the mutual arrangement of domains in the RNP particles is not strictly fixed suggesting that interaction with the third domain of the 30 S subunit is a requisite for their correct fitting.
authors.affiliation: Institute of Protein Research, Pushchino, Moscow Region, 142292, Russia. serdyuk@vega.protres.ru
authors.forename: I
authors.initials: I
authors.lastname: Serdyuk
authors.forename: A
authors.initials: A
authors.lastname: Ulitin
authors.forename: I
authors.initials: I
authors.lastname: Kolesnikov
authors.forename: V
authors.initials: V
authors.lastname: Vasiliev
authors.forename: V
authors.initials: V
authors.lastname: Aksenov
authors.forename: G
authors.initials: G
authors.lastname: Zaccai
authors.forename: D
authors.initials: D
authors.lastname: Svergun
authors.forename: M
authors.initials: M
authors.lastname: Kozin
authors.forename: R
authors.initials: R
authors.lastname: Willumeit
mesh_terms: D003198:Computer Simulation; D008854:Microscopy, Electron; D009502:Neutrons; D016914:Ribonuclease H; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000648:ultrastructure; D012270:Ribosomes / Q000737:chemistry*; D012542:Scattering, Radiation; D016963:Thermus thermophilus / Q000737:chemistry*; D014461:Ultracentrifugation
chemical_list: D012261:Ribonucleoproteins; D016914:Ribonuclease H