Book Chapter10.1016/0076-6879(79)59120-4
Neutron-scattering measurement of protein pair scattering functions from ribosomes containing deuterated proteins.
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TL;DR: This chapter discusses the methods used to obtain the neutron-scattering functions from the two ribosome mixtures used in the difference measurement and to derive the interference cross term for interpretation.
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Abstract: Publisher Summary This chapter discusses the methods used to obtain the neutron-scattering functions from the two ribosome mixtures used in the difference measurement and to derive the interference cross term for interpretation. The principal elements of the procedure are the loading of samples into cells for analysis, the setup of the experiment at the reactor facility, the protocol used for data collection, and the processing of data to obtain the final scattering curves. Although the specific characteristics of the ribosome system dictate many of the conditions used, a number of other specimens can be investigated using similar procedures. This is particularly true of the setup, data collection, and processing protocols. The successful measurement of pair interference functions is facilitated by the use of the highest possible sample concentration. A procedure is devised for centrifuging the ribosomal samples into the cells that are used in the scattering experiment. This required the development of appropriate adaptors for centrifugation and the development of cells and cell holders that are compatible both with the biochemistry of the sample and the mechanical requirements of the experiment.
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Citations
Positions of S2, S13, S16, S17, S19 and S21 in the 30 S ribosomal subunit of Escherichia coli.
M.S. Capel,M.S. Capel,M. Kjeldgaard,Donald M. Engelman,Donald M. Engelman,Peter B. Moore,Peter B. Moore +6 more
TL;DR: Neutron scattering distance data are presented for 33 protein pairs in the 30 S ribosomal subunit from Escherichia coli, along with the methods used for measuring distances between its exchangeable components as mentioned in this paper.
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X-ray and neutron small angle scattering
Bernard Jacrot
- 01 Jan 1982
TL;DR: When radiation (light, electrons, x-rays, neutrons) passes through matter, the inhomogeneities of density induce its scattering as mentioned in this paper, which makes objects visible through different optical properties from that of the surrounding medium.
93
Positions of proteins S14, S18 and S20 in the 30 S ribosomal subunit of Escherichia coli.
Venki Ramakrishnan,Venki Ramakrishnan,M.S. Capel,M.S. Capel,M. Kjeldgaard,M. Kjeldgaard,Donald M. Engelman,Donald M. Engelman,Peter B. Moore,Peter B. Moore +9 more
TL;DR: A map of the 30 S ribosomal subunit is presented giving the positions of 15 of its 21 proteins.
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Positions of proteins S6, S11 and S15 in the 30 S ribosomal subunit of Escherichia coli
Venki Ramakrishnan,Venki Ramakrishnan,S. Yabuki,S. Yabuki,I.-Y. Sillers,I.-Y. Sillers,D.G. Schindler,D.G. Schindler,Donald M. Engelman,Donald M. Engelman,Peter B. Moore,Peter B. Moore +11 more
TL;DR: It appears that many ribosomal proteins have compact configurations in the particles of Escherichia coli.
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Conformational changes of troponin C within the thin filaments detected by neutron scattering.
TL;DR: The in situ structure of TnC within the thin filaments was investigated with neutron scattering, combined with selective deuteration and the contrast matching technique, and radial movement of TNC by 4A is associated with large conformational changes of the entire Tn molecule by binding of Ca2+.
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References
A Two-Dimensional Position-Sensitive Detector for Thermal Neutrons
TL;DR: In this paper, a thermal neutron, two-dimensional position-sensitive detector for use in neutron scattering from biological samples was developed and tested. The detector is based on a multi-wire proportional concept with a gas filling of 6 atmos.
Triangulation of Proteins in the 30 S Ribosomal Subunit of Escherichia coli
Peter B. Moore,Peter B. Moore,Jerome A. Langer,Benno P. Schoenborn,D.M. Engelaman,D.M. Engelaman +5 more
TL;DR: Thermal neutron radiation has been used for solution scattering experiments on 30 S ribosomal subunits in which specific proteins have been inserted in deuterated form by reconstitution and the data support the view that many of these proteins are elongated.
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Neutron-scattering studies of the ribosome of Escherichia coli: a provisional map of the locations of proteins S3, S4, S5, S7, S8 and S9 in the 30 S subunit.
TL;DR: Results of neutron-scattering experiments to determine the distances between seven pairs of proteins within the 30 S ribosomal subunit lead to the construction of a three-dimensional map of the positions of the centers of mass of proteins S3, S4, S5, S7, S8 and S9.
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